Potassium in PDB 6naq: Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form
Enzymatic activity of Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form
All present enzymatic activity of Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form:
3.4.21.92;
Protein crystallography data
The structure of Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form, PDB code: 6naq
was solved by
W.A.Houry,
M.F.Mabanglo,
E.F.Pai,
B.T.Eger,
S.Bryson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
51.39 /
2.02
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
98.584,
127.945,
120.195,
90.00,
90.19,
90.00
|
R / Rfree (%)
|
20.7 /
24.6
|
Potassium Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
14;
Binding sites:
The binding sites of Potassium atom in the Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form
(pdb code 6naq). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 14 binding sites of Potassium where determined in the
Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form, PDB code: 6naq:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Potassium binding site 1 out
of 14 in 6naq
Go back to
Potassium Binding Sites List in 6naq
Potassium binding site 1 out
of 14 in the Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K301
b:15.5
occ:1.00
|
O
|
A:MET85
|
2.7
|
16.8
|
1.0
|
O
|
A:HOH435
|
2.8
|
16.6
|
1.0
|
O
|
A:PRO90
|
2.8
|
17.7
|
1.0
|
O
|
A:ILE88
|
2.8
|
16.0
|
1.0
|
O
|
A:HOH437
|
2.9
|
14.7
|
1.0
|
C
|
A:PRO90
|
3.7
|
19.9
|
1.0
|
C
|
A:ILE88
|
3.9
|
21.3
|
1.0
|
C
|
A:MET85
|
3.9
|
21.9
|
1.0
|
O
|
A:LYS89
|
3.9
|
19.4
|
1.0
|
O
|
A:HOH454
|
4.0
|
12.9
|
1.0
|
CG1
|
A:ILE88
|
4.1
|
18.2
|
1.0
|
O
|
A:ASN86
|
4.1
|
22.2
|
1.0
|
C
|
A:LYS89
|
4.2
|
13.9
|
1.0
|
C
|
A:ASN86
|
4.3
|
21.9
|
1.0
|
CA
|
A:ASN86
|
4.3
|
22.7
|
1.0
|
CA
|
A:ASP91
|
4.4
|
20.7
|
1.0
|
N
|
A:ASP91
|
4.4
|
17.7
|
1.0
|
N
|
A:VAL92
|
4.5
|
16.5
|
1.0
|
OE1
|
A:GLU112
|
4.5
|
21.2
|
1.0
|
N
|
A:ILE88
|
4.6
|
17.6
|
1.0
|
N
|
A:ASN86
|
4.6
|
17.5
|
1.0
|
CG2
|
A:VAL92
|
4.7
|
16.1
|
1.0
|
N
|
A:PRO90
|
4.7
|
16.5
|
1.0
|
O
|
A:HOH433
|
4.7
|
18.6
|
1.0
|
CA
|
A:ILE88
|
4.7
|
17.9
|
1.0
|
CA
|
A:PRO90
|
4.8
|
17.4
|
1.0
|
N
|
A:LYS89
|
4.8
|
21.4
|
1.0
|
CA
|
A:LYS89
|
4.8
|
14.3
|
1.0
|
C
|
A:ASP91
|
4.8
|
20.5
|
1.0
|
N
|
A:PHE87
|
5.0
|
18.4
|
1.0
|
|
Potassium binding site 2 out
of 14 in 6naq
Go back to
Potassium Binding Sites List in 6naq
Potassium binding site 2 out
of 14 in the Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K301
b:20.7
occ:1.00
|
O
|
B:MET85
|
2.7
|
19.5
|
1.0
|
O
|
B:PRO90
|
2.7
|
18.7
|
1.0
|
O
|
B:HOH422
|
2.8
|
14.2
|
1.0
|
O
|
B:HOH445
|
2.8
|
16.4
|
1.0
|
O
|
B:ILE88
|
2.8
|
19.0
|
1.0
|
O
|
B:HOH409
|
2.9
|
21.9
|
1.0
|
C
|
B:PRO90
|
3.8
|
25.3
|
1.0
|
C
|
B:MET85
|
3.9
|
21.0
|
1.0
|
C
|
B:ILE88
|
3.9
|
21.4
|
1.0
|
O
|
B:LYS89
|
4.1
|
19.7
|
1.0
|
CG1
|
B:ILE88
|
4.1
|
15.0
|
1.0
|
O
|
B:HOH453
|
4.2
|
20.4
|
1.0
|
O
|
B:ASN86
|
4.2
|
22.1
|
1.0
|
CA
|
B:ASN86
|
4.3
|
18.9
|
1.0
|
CA
|
B:ASP91
|
4.3
|
19.8
|
1.0
|
C
|
B:LYS89
|
4.4
|
17.1
|
1.0
|
C
|
B:ASN86
|
4.4
|
22.1
|
1.0
|
N
|
B:VAL92
|
4.4
|
20.6
|
1.0
|
N
|
B:ASP91
|
4.4
|
19.4
|
1.0
|
OE1
|
B:GLU112
|
4.4
|
24.2
|
1.0
|
O
|
B:HOH447
|
4.4
|
29.9
|
1.0
|
N
|
B:ASN86
|
4.6
|
16.9
|
1.0
|
O
|
B:HOH441
|
4.6
|
18.1
|
1.0
|
CG2
|
B:VAL92
|
4.6
|
16.7
|
1.0
|
N
|
B:ILE88
|
4.7
|
17.6
|
1.0
|
N
|
B:PRO90
|
4.7
|
17.8
|
1.0
|
C
|
B:ASP91
|
4.7
|
19.3
|
1.0
|
CA
|
B:ILE88
|
4.8
|
21.2
|
1.0
|
N
|
B:LYS89
|
4.8
|
21.3
|
1.0
|
CA
|
B:PRO90
|
4.8
|
18.4
|
1.0
|
CA
|
B:LYS89
|
4.9
|
21.9
|
1.0
|
CA
|
B:MET85
|
5.0
|
20.8
|
1.0
|
|
Potassium binding site 3 out
of 14 in 6naq
Go back to
Potassium Binding Sites List in 6naq
Potassium binding site 3 out
of 14 in the Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K301
b:18.8
occ:1.00
|
O
|
C:MET85
|
2.7
|
16.4
|
1.0
|
O
|
C:PRO90
|
2.7
|
17.0
|
1.0
|
O
|
C:ILE88
|
2.8
|
16.8
|
1.0
|
O
|
C:HOH421
|
2.8
|
17.5
|
1.0
|
O
|
C:HOH407
|
2.9
|
15.4
|
1.0
|
C
|
C:PRO90
|
3.7
|
23.5
|
1.0
|
C
|
C:MET85
|
3.9
|
21.5
|
1.0
|
C
|
C:ILE88
|
3.9
|
18.1
|
1.0
|
CG1
|
C:ILE88
|
4.0
|
17.2
|
1.0
|
O
|
C:LYS89
|
4.1
|
18.0
|
1.0
|
CA
|
C:ASP91
|
4.3
|
18.1
|
1.0
|
C
|
C:LYS89
|
4.3
|
18.3
|
1.0
|
O
|
C:HOH445
|
4.3
|
11.6
|
1.0
|
O
|
C:ASN86
|
4.3
|
23.6
|
1.0
|
N
|
C:ASP91
|
4.3
|
16.3
|
1.0
|
N
|
C:VAL92
|
4.3
|
17.5
|
1.0
|
CA
|
C:ASN86
|
4.4
|
17.5
|
1.0
|
C
|
C:ASN86
|
4.4
|
14.5
|
1.0
|
OE1
|
C:GLU112
|
4.5
|
22.5
|
1.0
|
O
|
C:HOH434
|
4.6
|
15.6
|
1.0
|
CG2
|
C:VAL92
|
4.6
|
15.0
|
1.0
|
N
|
C:ASN86
|
4.6
|
17.9
|
1.0
|
N
|
C:PRO90
|
4.6
|
16.8
|
1.0
|
C
|
C:ASP91
|
4.7
|
21.1
|
1.0
|
N
|
C:ILE88
|
4.7
|
19.8
|
1.0
|
CA
|
C:PRO90
|
4.7
|
16.4
|
1.0
|
CA
|
C:ILE88
|
4.7
|
16.9
|
1.0
|
N
|
C:LYS89
|
4.8
|
18.4
|
1.0
|
CA
|
C:LYS89
|
4.9
|
18.9
|
1.0
|
CA
|
C:MET85
|
5.0
|
16.9
|
1.0
|
|
Potassium binding site 4 out
of 14 in 6naq
Go back to
Potassium Binding Sites List in 6naq
Potassium binding site 4 out
of 14 in the Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K301
b:22.4
occ:1.00
|
O
|
D:PRO90
|
2.7
|
24.0
|
1.0
|
O
|
D:MET85
|
2.7
|
19.5
|
1.0
|
O
|
D:HOH439
|
2.7
|
25.9
|
1.0
|
O
|
D:HOH427
|
2.8
|
26.0
|
1.0
|
O
|
D:ILE88
|
3.0
|
21.9
|
1.0
|
O
|
D:HOH411
|
3.0
|
15.6
|
1.0
|
C
|
D:PRO90
|
3.7
|
23.3
|
1.0
|
O
|
D:HOH428
|
3.9
|
24.2
|
1.0
|
C
|
D:MET85
|
3.9
|
24.8
|
1.0
|
C
|
D:ILE88
|
4.0
|
21.6
|
1.0
|
O
|
D:LYS89
|
4.1
|
22.9
|
1.0
|
CG1
|
D:ILE88
|
4.1
|
17.3
|
1.0
|
O
|
D:ASN86
|
4.1
|
22.0
|
1.0
|
O
|
D:HOH441
|
4.1
|
19.0
|
1.0
|
CA
|
D:ASP91
|
4.3
|
21.8
|
1.0
|
C
|
D:ASN86
|
4.3
|
26.5
|
1.0
|
CG2
|
D:VAL92
|
4.3
|
14.9
|
1.0
|
N
|
D:VAL92
|
4.3
|
19.8
|
1.0
|
CA
|
D:ASN86
|
4.3
|
21.0
|
1.0
|
N
|
D:ASP91
|
4.4
|
18.6
|
1.0
|
C
|
D:LYS89
|
4.4
|
18.0
|
1.0
|
OE1
|
D:GLU112
|
4.4
|
26.0
|
1.0
|
N
|
D:ASN86
|
4.6
|
20.9
|
1.0
|
C
|
D:ASP91
|
4.7
|
23.4
|
1.0
|
O
|
D:HOH413
|
4.7
|
22.9
|
1.0
|
N
|
D:ILE88
|
4.7
|
23.5
|
1.0
|
N
|
D:PRO90
|
4.7
|
16.6
|
1.0
|
CA
|
D:PRO90
|
4.8
|
17.2
|
1.0
|
CA
|
D:ILE88
|
4.8
|
22.9
|
1.0
|
N
|
D:LYS89
|
4.9
|
20.5
|
1.0
|
CA
|
D:LYS89
|
5.0
|
20.6
|
1.0
|
|
Potassium binding site 5 out
of 14 in 6naq
Go back to
Potassium Binding Sites List in 6naq
Potassium binding site 5 out
of 14 in the Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 5 of Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K301
b:33.1
occ:1.00
|
O
|
E:MET85
|
2.6
|
22.5
|
1.0
|
O
|
E:ILE88
|
2.7
|
22.9
|
1.0
|
O
|
E:PRO90
|
2.8
|
27.0
|
1.0
|
O
|
E:HOH424
|
2.8
|
41.4
|
1.0
|
O
|
E:HOH404
|
3.0
|
14.7
|
1.0
|
O
|
E:HOH402
|
3.2
|
25.4
|
1.0
|
C
|
E:ILE88
|
3.8
|
22.6
|
1.0
|
C
|
E:PRO90
|
3.8
|
25.8
|
1.0
|
C
|
E:MET85
|
3.8
|
25.1
|
1.0
|
CG1
|
E:ILE88
|
3.9
|
22.0
|
1.0
|
O
|
E:LYS89
|
4.1
|
27.5
|
1.0
|
C
|
E:LYS89
|
4.3
|
22.0
|
1.0
|
O
|
E:ASN86
|
4.3
|
26.3
|
1.0
|
CA
|
E:ASN86
|
4.3
|
22.9
|
1.0
|
C
|
E:ASN86
|
4.3
|
23.0
|
1.0
|
CA
|
E:ASP91
|
4.3
|
23.8
|
1.0
|
N
|
E:VAL92
|
4.4
|
20.2
|
1.0
|
OE1
|
E:GLU112
|
4.4
|
25.2
|
1.0
|
N
|
E:ASP91
|
4.4
|
21.9
|
1.0
|
N
|
E:ASN86
|
4.5
|
23.6
|
1.0
|
CG2
|
E:VAL92
|
4.5
|
16.4
|
1.0
|
N
|
E:ILE88
|
4.5
|
24.3
|
1.0
|
CA
|
E:ILE88
|
4.6
|
23.9
|
1.0
|
N
|
E:LYS89
|
4.6
|
26.3
|
1.0
|
N
|
E:PRO90
|
4.7
|
22.7
|
1.0
|
CA
|
E:LYS89
|
4.7
|
21.0
|
1.0
|
C
|
E:ASP91
|
4.7
|
26.1
|
1.0
|
CD1
|
E:ILE88
|
4.9
|
19.3
|
1.0
|
CA
|
E:PRO90
|
4.9
|
21.4
|
1.0
|
CB
|
E:ILE88
|
4.9
|
21.6
|
1.0
|
N
|
E:PHE87
|
5.0
|
20.4
|
1.0
|
CA
|
E:MET85
|
5.0
|
21.1
|
1.0
|
|
Potassium binding site 6 out
of 14 in 6naq
Go back to
Potassium Binding Sites List in 6naq
Potassium binding site 6 out
of 14 in the Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 6 of Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:K301
b:29.0
occ:1.00
|
O
|
F:PRO90
|
2.7
|
22.4
|
1.0
|
O
|
F:HOH417
|
2.7
|
27.0
|
1.0
|
O
|
F:MET85
|
2.7
|
24.6
|
1.0
|
O
|
F:ILE88
|
2.7
|
20.0
|
1.0
|
O
|
F:HOH432
|
2.9
|
26.8
|
1.0
|
O
|
F:HOH420
|
3.0
|
26.8
|
1.0
|
C
|
F:PRO90
|
3.7
|
25.8
|
1.0
|
C
|
F:ILE88
|
3.8
|
21.4
|
1.0
|
C
|
F:MET85
|
3.9
|
23.3
|
1.0
|
O
|
F:LYS89
|
4.0
|
23.0
|
1.0
|
CG1
|
F:ILE88
|
4.1
|
19.4
|
1.0
|
O
|
F:HOH437
|
4.1
|
21.8
|
1.0
|
O
|
F:ASN86
|
4.1
|
25.2
|
1.0
|
C
|
F:LYS89
|
4.2
|
15.4
|
1.0
|
C
|
F:ASN86
|
4.3
|
23.1
|
1.0
|
CA
|
F:ASN86
|
4.3
|
23.0
|
1.0
|
CA
|
F:ASP91
|
4.3
|
21.6
|
1.0
|
N
|
F:ASP91
|
4.4
|
19.6
|
1.0
|
N
|
F:VAL92
|
4.5
|
22.8
|
1.0
|
N
|
F:ASN86
|
4.6
|
21.4
|
1.0
|
N
|
F:PRO90
|
4.6
|
20.2
|
1.0
|
OE1
|
F:GLU112
|
4.6
|
29.2
|
1.0
|
N
|
F:ILE88
|
4.6
|
17.9
|
1.0
|
CA
|
F:ILE88
|
4.7
|
18.0
|
1.0
|
N
|
F:LYS89
|
4.7
|
25.6
|
1.0
|
O
|
F:HOH422
|
4.7
|
23.7
|
1.0
|
CA
|
F:PRO90
|
4.8
|
15.4
|
1.0
|
C
|
F:ASP91
|
4.8
|
24.9
|
1.0
|
CA
|
F:LYS89
|
4.8
|
22.8
|
1.0
|
CG2
|
F:VAL92
|
4.9
|
19.5
|
1.0
|
OD1
|
F:ASP91
|
5.0
|
21.1
|
1.0
|
|
Potassium binding site 7 out
of 14 in 6naq
Go back to
Potassium Binding Sites List in 6naq
Potassium binding site 7 out
of 14 in the Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 7 of Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:K301
b:18.7
occ:1.00
|
O
|
G:MET85
|
2.7
|
18.2
|
1.0
|
O
|
G:PRO90
|
2.7
|
20.7
|
1.0
|
O
|
G:HOH443
|
2.8
|
15.8
|
1.0
|
O
|
G:ILE88
|
2.8
|
16.5
|
1.0
|
O
|
G:HOH427
|
2.9
|
15.3
|
1.0
|
O
|
G:HOH415
|
3.5
|
27.1
|
1.0
|
C
|
G:PRO90
|
3.8
|
23.9
|
1.0
|
C
|
G:MET85
|
3.9
|
22.1
|
1.0
|
C
|
G:ILE88
|
3.9
|
21.4
|
1.0
|
O
|
G:HOH449
|
4.0
|
8.9
|
1.0
|
O
|
G:ASN86
|
4.1
|
21.6
|
1.0
|
CG1
|
G:ILE88
|
4.1
|
16.9
|
1.0
|
O
|
G:LYS89
|
4.2
|
14.1
|
1.0
|
C
|
G:ASN86
|
4.2
|
24.3
|
1.0
|
CA
|
G:ASN86
|
4.3
|
21.7
|
1.0
|
C
|
G:LYS89
|
4.4
|
16.2
|
1.0
|
CA
|
G:ASP91
|
4.4
|
20.5
|
1.0
|
OE1
|
G:GLU112
|
4.4
|
18.6
|
1.0
|
N
|
G:ASP91
|
4.4
|
20.2
|
1.0
|
N
|
G:VAL92
|
4.5
|
16.1
|
1.0
|
CG2
|
G:VAL92
|
4.5
|
13.2
|
1.0
|
N
|
G:ILE88
|
4.5
|
20.9
|
1.0
|
N
|
G:ASN86
|
4.6
|
17.9
|
1.0
|
N
|
G:PRO90
|
4.7
|
15.3
|
1.0
|
CA
|
G:ILE88
|
4.7
|
20.9
|
1.0
|
C
|
G:ASP91
|
4.8
|
21.6
|
1.0
|
CA
|
G:PRO90
|
4.8
|
13.8
|
1.0
|
N
|
G:LYS89
|
4.9
|
18.5
|
1.0
|
N
|
G:PHE87
|
4.9
|
21.7
|
1.0
|
CA
|
G:LYS89
|
4.9
|
19.9
|
1.0
|
|
Potassium binding site 8 out
of 14 in 6naq
Go back to
Potassium Binding Sites List in 6naq
Potassium binding site 8 out
of 14 in the Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 8 of Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:K301
b:28.2
occ:1.00
|
O
|
H:MET85
|
2.7
|
23.2
|
1.0
|
O
|
H:HOH418
|
2.8
|
19.3
|
1.0
|
O
|
H:PRO90
|
2.8
|
21.9
|
1.0
|
O
|
H:ILE88
|
2.9
|
19.1
|
1.0
|
O
|
H:HOH402
|
2.9
|
24.1
|
1.0
|
C
|
H:PRO90
|
3.8
|
21.4
|
1.0
|
C
|
H:MET85
|
3.9
|
25.9
|
1.0
|
C
|
H:ILE88
|
4.0
|
20.7
|
1.0
|
O
|
H:LYS89
|
4.0
|
20.1
|
1.0
|
CG1
|
H:ILE88
|
4.1
|
21.0
|
1.0
|
O
|
H:ASN86
|
4.2
|
26.3
|
1.0
|
CA
|
H:ASP91
|
4.3
|
22.1
|
1.0
|
C
|
H:ASN86
|
4.3
|
23.5
|
1.0
|
N
|
H:VAL92
|
4.3
|
23.4
|
1.0
|
C
|
H:LYS89
|
4.3
|
20.0
|
1.0
|
CA
|
H:ASN86
|
4.4
|
25.0
|
1.0
|
N
|
H:ASP91
|
4.4
|
18.6
|
1.0
|
OE1
|
H:GLU112
|
4.5
|
26.4
|
1.0
|
CG2
|
H:VAL92
|
4.5
|
18.0
|
1.0
|
N
|
H:ASN86
|
4.6
|
23.4
|
1.0
|
N
|
H:ILE88
|
4.7
|
22.4
|
1.0
|
C
|
H:ASP91
|
4.7
|
22.2
|
1.0
|
N
|
H:PRO90
|
4.8
|
18.5
|
1.0
|
CA
|
H:ILE88
|
4.8
|
20.3
|
1.0
|
N
|
H:LYS89
|
4.9
|
23.9
|
1.0
|
CA
|
H:LYS89
|
4.9
|
22.7
|
1.0
|
CA
|
H:PRO90
|
4.9
|
21.0
|
1.0
|
CA
|
H:MET85
|
5.0
|
23.0
|
1.0
|
|
Potassium binding site 9 out
of 14 in 6naq
Go back to
Potassium Binding Sites List in 6naq
Potassium binding site 9 out
of 14 in the Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 9 of Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:K301
b:33.5
occ:1.00
|
O
|
I:PRO90
|
2.6
|
27.2
|
1.0
|
O
|
I:MET85
|
2.6
|
26.1
|
1.0
|
O
|
I:ILE88
|
2.7
|
22.1
|
1.0
|
O
|
I:HOH416
|
2.8
|
25.7
|
1.0
|
O
|
I:HOH426
|
3.1
|
41.3
|
1.0
|
C
|
I:PRO90
|
3.7
|
26.0
|
1.0
|
C
|
I:MET85
|
3.8
|
26.5
|
1.0
|
C
|
I:ILE88
|
3.9
|
23.9
|
1.0
|
CG1
|
I:ILE88
|
4.0
|
20.8
|
1.0
|
O
|
I:HOH424
|
4.0
|
30.8
|
1.0
|
O
|
I:LYS89
|
4.1
|
26.8
|
1.0
|
O
|
I:HOH428
|
4.2
|
37.5
|
1.0
|
CA
|
I:ASP91
|
4.2
|
23.1
|
1.0
|
O
|
I:ASN86
|
4.3
|
26.0
|
1.0
|
C
|
I:LYS89
|
4.3
|
20.9
|
1.0
|
N
|
I:ASP91
|
4.3
|
18.9
|
1.0
|
CA
|
I:ASN86
|
4.4
|
24.6
|
1.0
|
C
|
I:ASN86
|
4.4
|
24.4
|
1.0
|
N
|
I:VAL92
|
4.4
|
25.4
|
1.0
|
OE1
|
I:GLU112
|
4.5
|
29.2
|
1.0
|
CG2
|
I:VAL92
|
4.6
|
15.7
|
1.0
|
N
|
I:ASN86
|
4.6
|
23.6
|
1.0
|
N
|
I:ILE88
|
4.6
|
26.8
|
1.0
|
N
|
I:PRO90
|
4.6
|
21.7
|
1.0
|
C
|
I:ASP91
|
4.7
|
25.1
|
1.0
|
CA
|
I:ILE88
|
4.7
|
24.5
|
1.0
|
N
|
I:LYS89
|
4.8
|
24.1
|
1.0
|
CA
|
I:PRO90
|
4.8
|
20.8
|
1.0
|
O
|
I:HOH418
|
4.8
|
27.0
|
1.0
|
CA
|
I:LYS89
|
4.8
|
19.1
|
1.0
|
CD1
|
I:ILE88
|
4.9
|
19.0
|
1.0
|
CA
|
I:MET85
|
4.9
|
20.5
|
1.0
|
CB
|
I:ILE88
|
5.0
|
19.9
|
1.0
|
OD1
|
I:ASP91
|
5.0
|
22.2
|
1.0
|
|
Potassium binding site 10 out
of 14 in 6naq
Go back to
Potassium Binding Sites List in 6naq
Potassium binding site 10 out
of 14 in the Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 10 of Crystal Structure of Neisseria Meningitidis Clpp Protease in Apo Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:K301
b:17.1
occ:1.00
|
O
|
J:MET85
|
2.6
|
16.2
|
1.0
|
O
|
J:PRO90
|
2.7
|
21.2
|
1.0
|
O
|
J:HOH430
|
2.8
|
21.0
|
1.0
|
O
|
J:HOH410
|
2.8
|
17.9
|
1.0
|
O
|
J:ILE88
|
3.0
|
16.0
|
1.0
|
C
|
J:PRO90
|
3.8
|
22.5
|
1.0
|
O
|
J:HOH412
|
3.8
|
29.7
|
1.0
|
C
|
J:MET85
|
3.8
|
24.4
|
1.0
|
C
|
J:ILE88
|
4.0
|
20.5
|
1.0
|
CG1
|
J:ILE88
|
4.1
|
19.0
|
1.0
|
O
|
J:LYS89
|
4.1
|
20.3
|
1.0
|
O
|
J:HOH444
|
4.1
|
14.2
|
1.0
|
O
|
J:ASN86
|
4.3
|
21.8
|
1.0
|
C
|
J:ASN86
|
4.3
|
25.4
|
1.0
|
OE1
|
J:GLU112
|
4.3
|
18.2
|
1.0
|
CA
|
J:ASN86
|
4.3
|
23.0
|
1.0
|
CA
|
J:ASP91
|
4.3
|
19.3
|
1.0
|
C
|
J:LYS89
|
4.4
|
20.6
|
1.0
|
N
|
J:VAL92
|
4.4
|
17.1
|
1.0
|
N
|
J:ASP91
|
4.4
|
17.4
|
1.0
|
CG2
|
J:VAL92
|
4.5
|
12.2
|
1.0
|
O
|
J:HOH428
|
4.6
|
19.3
|
1.0
|
N
|
J:ASN86
|
4.6
|
18.6
|
1.0
|
N
|
J:ILE88
|
4.7
|
19.4
|
1.0
|
N
|
J:PRO90
|
4.7
|
15.4
|
1.0
|
C
|
J:ASP91
|
4.8
|
20.6
|
1.0
|
CA
|
J:ILE88
|
4.8
|
23.0
|
1.0
|
CA
|
J:PRO90
|
4.8
|
17.4
|
1.0
|
CA
|
J:MET85
|
4.9
|
18.4
|
1.0
|
N
|
J:LYS89
|
4.9
|
21.6
|
1.0
|
N
|
J:PHE87
|
5.0
|
21.3
|
1.0
|
|
Reference:
M.F.Mabanglo,
W.A.Houry.
Molecular Basis of Clpp Activation By Small Molecules To Be Published.
Page generated: Mon Aug 12 16:57:52 2024
|