Potassium in PDB 1r64: The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor
Enzymatic activity of The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor
All present enzymatic activity of The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor:
3.4.21.61;
Protein crystallography data
The structure of The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor, PDB code: 1r64
was solved by
T.Holyoak,
C.A.Kettner,
G.A.Petsko,
R.S.Fuller,
D.Ringe,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
2.20
|
Space group
|
P 65 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
113.541,
113.541,
364.971,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
19.7 /
23.4
|
Other elements in 1r64:
The structure of The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor
(pdb code 1r64). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 6 binding sites of Potassium where determined in the
The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor, PDB code: 1r64:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
Potassium binding site 1 out
of 6 in 1r64
Go back to
Potassium Binding Sites List in 1r64
Potassium binding site 1 out
of 6 in the The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K800
b:31.7
occ:1.00
|
OH
|
A:TYR261
|
2.6
|
26.6
|
1.0
|
O
|
A:SER194
|
2.7
|
22.9
|
1.0
|
O
|
A:GLU192
|
2.8
|
28.7
|
1.0
|
O
|
A:ALA191
|
2.9
|
25.6
|
1.0
|
C
|
A:GLU192
|
3.4
|
27.7
|
1.0
|
O
|
A:HOH1187
|
3.6
|
41.9
|
1.0
|
CZ
|
A:TYR261
|
3.7
|
26.1
|
1.0
|
CA
|
A:GLU192
|
3.7
|
27.5
|
1.0
|
C
|
A:SER194
|
3.8
|
23.1
|
1.0
|
CE2
|
A:TYR261
|
3.9
|
27.3
|
1.0
|
C
|
A:ALA191
|
3.9
|
25.3
|
1.0
|
N
|
A:SER194
|
3.9
|
22.4
|
1.0
|
O
|
A:HOH1006
|
4.1
|
27.8
|
1.0
|
N
|
A:GLU192
|
4.3
|
26.2
|
1.0
|
N
|
A:GLY193
|
4.4
|
26.1
|
1.0
|
CA
|
A:SER194
|
4.4
|
22.3
|
1.0
|
O
|
A:HOH1288
|
4.5
|
41.4
|
1.0
|
CE3
|
A:TRP195
|
4.6
|
26.6
|
1.0
|
O
|
A:HOH1037
|
4.6
|
35.3
|
1.0
|
O
|
A:ASN202
|
4.8
|
32.8
|
1.0
|
C
|
A:GLY193
|
4.8
|
24.6
|
1.0
|
CA
|
A:GLY193
|
4.9
|
25.4
|
1.0
|
CB
|
A:ASN202
|
4.9
|
37.1
|
1.0
|
N
|
A:TRP195
|
4.9
|
23.6
|
1.0
|
CE1
|
A:TYR261
|
4.9
|
25.0
|
1.0
|
|
Potassium binding site 2 out
of 6 in 1r64
Go back to
Potassium Binding Sites List in 1r64
Potassium binding site 2 out
of 6 in the The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K801
b:36.2
occ:1.00
|
O
|
A:TRP467
|
2.6
|
22.5
|
1.0
|
O
|
A:ALA500
|
2.8
|
24.9
|
1.0
|
O
|
A:HOH1221
|
2.8
|
31.0
|
1.0
|
OG1
|
A:THR466
|
3.0
|
20.7
|
1.0
|
O
|
A:HOH1228
|
3.2
|
36.6
|
1.0
|
C
|
A:TRP467
|
3.7
|
23.4
|
1.0
|
C
|
A:ALA500
|
3.8
|
25.4
|
1.0
|
O
|
A:HOH1236
|
3.9
|
37.5
|
1.0
|
N
|
A:TRP467
|
3.9
|
20.1
|
1.0
|
CB
|
A:ALA500
|
4.0
|
27.0
|
1.0
|
CA
|
A:ALA500
|
4.2
|
25.8
|
1.0
|
CB
|
A:THR466
|
4.3
|
21.0
|
1.0
|
CA
|
A:TRP467
|
4.4
|
21.8
|
1.0
|
CG2
|
A:THR466
|
4.6
|
20.0
|
1.0
|
O
|
A:HOH1208
|
4.7
|
34.4
|
1.0
|
N
|
A:PHE468
|
4.8
|
21.9
|
1.0
|
CD1
|
A:TRP467
|
4.9
|
23.7
|
1.0
|
C
|
A:THR466
|
5.0
|
21.8
|
1.0
|
|
Potassium binding site 3 out
of 6 in 1r64
Go back to
Potassium Binding Sites List in 1r64
Potassium binding site 3 out
of 6 in the The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K802
b:36.1
occ:1.00
|
O
|
A:LEU246
|
2.7
|
25.8
|
1.0
|
O
|
A:HOH1244
|
2.9
|
35.4
|
1.0
|
O
|
B:HOH1920
|
2.9
|
19.8
|
1.0
|
O
|
B:HOH2043
|
3.0
|
25.4
|
1.0
|
O
|
B:HOH2002
|
3.0
|
21.5
|
1.0
|
O
|
C:HOH988
|
3.0
|
41.2
|
1.0
|
O
|
C:HOH465
|
3.5
|
16.9
|
1.0
|
C
|
A:LEU246
|
3.9
|
24.9
|
1.0
|
O
|
A:HOH993
|
4.1
|
18.7
|
1.0
|
OD1
|
B:ASP431
|
4.1
|
23.5
|
1.0
|
CE
|
C:LYS4
|
4.2
|
20.2
|
1.0
|
O
|
B:HOH2116
|
4.4
|
32.1
|
1.0
|
NZ
|
B:LYS437
|
4.5
|
14.9
|
1.0
|
OD2
|
B:ASP431
|
4.6
|
19.6
|
1.0
|
N
|
A:GLY248
|
4.6
|
30.5
|
1.0
|
CB
|
A:LEU246
|
4.7
|
21.0
|
1.0
|
CA
|
A:LEU246
|
4.7
|
23.0
|
1.0
|
CG
|
B:ASP431
|
4.8
|
19.6
|
1.0
|
N
|
A:SER247
|
4.8
|
25.4
|
1.0
|
CA
|
A:SER247
|
4.8
|
27.5
|
1.0
|
NZ
|
C:LYS4
|
4.8
|
19.4
|
1.0
|
OE1
|
C:GLU3
|
4.9
|
26.0
|
1.0
|
CD
|
B:LYS437
|
4.9
|
17.6
|
1.0
|
CE
|
B:LYS437
|
4.9
|
18.2
|
1.0
|
CD
|
C:LYS4
|
4.9
|
17.3
|
1.0
|
CG
|
C:LYS4
|
4.9
|
18.0
|
1.0
|
O
|
C:ARG2
|
5.0
|
23.2
|
1.0
|
|
Potassium binding site 4 out
of 6 in 1r64
Go back to
Potassium Binding Sites List in 1r64
Potassium binding site 4 out
of 6 in the The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K800
b:41.3
occ:1.00
|
O
|
B:SER194
|
2.7
|
32.0
|
1.0
|
OH
|
B:TYR261
|
2.7
|
32.7
|
1.0
|
O
|
B:ALA191
|
2.7
|
34.5
|
1.0
|
O
|
B:GLU192
|
3.0
|
35.5
|
1.0
|
C
|
B:GLU192
|
3.6
|
36.0
|
1.0
|
CZ
|
B:TYR261
|
3.8
|
31.2
|
1.0
|
C
|
B:SER194
|
3.8
|
31.6
|
1.0
|
CA
|
B:GLU192
|
3.8
|
37.0
|
1.0
|
C
|
B:ALA191
|
3.8
|
34.7
|
1.0
|
N
|
B:SER194
|
4.0
|
33.0
|
1.0
|
CE2
|
B:TYR261
|
4.0
|
29.8
|
1.0
|
O
|
B:HOH1930
|
4.1
|
30.3
|
1.0
|
N
|
B:GLU192
|
4.3
|
35.8
|
1.0
|
CA
|
B:SER194
|
4.4
|
32.1
|
1.0
|
N
|
B:GLY193
|
4.5
|
36.3
|
1.0
|
CE3
|
B:TRP195
|
4.5
|
39.1
|
1.0
|
O
|
B:ASN202
|
4.5
|
42.2
|
1.0
|
CB
|
B:ASN202
|
4.7
|
47.5
|
1.0
|
O
|
B:HOH1987
|
4.8
|
42.2
|
1.0
|
C
|
B:GLY193
|
4.9
|
34.7
|
1.0
|
N
|
B:TRP195
|
4.9
|
32.1
|
1.0
|
CB
|
B:SER194
|
5.0
|
31.2
|
1.0
|
|
Potassium binding site 5 out
of 6 in 1r64
Go back to
Potassium Binding Sites List in 1r64
Potassium binding site 5 out
of 6 in the The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 5 of The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K801
b:39.6
occ:1.00
|
O
|
B:ALA500
|
2.6
|
24.4
|
1.0
|
OG1
|
B:THR466
|
2.8
|
25.8
|
1.0
|
O
|
B:HOH2172
|
2.9
|
47.4
|
1.0
|
O
|
B:TRP467
|
3.0
|
24.8
|
1.0
|
O
|
B:HOH2176
|
3.0
|
29.8
|
1.0
|
O
|
B:HOH2175
|
3.1
|
59.2
|
1.0
|
O
|
B:HOH2174
|
3.6
|
38.9
|
1.0
|
C
|
B:ALA500
|
3.7
|
23.8
|
1.0
|
O
|
B:HOH2089
|
3.9
|
35.1
|
1.0
|
N
|
B:TRP467
|
4.1
|
21.1
|
1.0
|
C
|
B:TRP467
|
4.1
|
24.1
|
1.0
|
CB
|
B:THR466
|
4.2
|
23.8
|
1.0
|
CA
|
B:ALA500
|
4.2
|
24.4
|
1.0
|
CB
|
B:ALA500
|
4.2
|
23.5
|
1.0
|
CG2
|
B:THR466
|
4.5
|
21.4
|
1.0
|
CA
|
B:TRP467
|
4.8
|
23.7
|
1.0
|
CB
|
B:ASN501
|
4.8
|
21.1
|
1.0
|
N
|
B:ASN501
|
4.8
|
22.6
|
1.0
|
C
|
B:THR466
|
5.0
|
21.4
|
1.0
|
|
Potassium binding site 6 out
of 6 in 1r64
Go back to
Potassium Binding Sites List in 1r64
Potassium binding site 6 out
of 6 in the The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 6 of The 2.2 A Crystal Structure of KEX2 Protease in Complex with Ac-Arg- Glu-Lys-Boroarg Peptidyl Boronic Acid Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K803
b:69.4
occ:1.00
|
O
|
B:HOH2083
|
2.8
|
23.5
|
1.0
|
O
|
B:HOH1931
|
3.3
|
17.4
|
1.0
|
O
|
B:HOH1963
|
3.4
|
31.5
|
1.0
|
O
|
B:HOH2197
|
3.6
|
35.8
|
1.0
|
O
|
B:HOH1951
|
3.7
|
19.9
|
1.0
|
NH1
|
B:ARG441
|
3.8
|
25.9
|
1.0
|
O
|
B:HOH1953
|
4.4
|
20.2
|
1.0
|
CD
|
B:ARG441
|
4.9
|
26.1
|
1.0
|
CZ
|
B:ARG441
|
5.0
|
25.8
|
1.0
|
|
Reference:
T.Holyoak,
C.A.Kettner,
G.A.Petsko,
R.S.Fuller,
D.Ringe.
Structural Basis For Differences in Substrate Selectivity in KEX2 and Furin Protein Convertases Biochemistry V. 43 2412 2004.
ISSN: ISSN 0006-2960
PubMed: 14992578
DOI: 10.1021/BI035849H
Page generated: Mon Aug 12 05:16:43 2024
|