Potassium in PDB 5g0x: Pseudomonas Aeruginosa Hdah Bound to Acetate.
Protein crystallography data
The structure of Pseudomonas Aeruginosa Hdah Bound to Acetate., PDB code: 5g0x
was solved by
A.Kraemer,
F.J.Meyer-Almes,
O.Yildiz,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
75.69 /
1.70
|
Space group
|
P 41 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
81.390,
81.390,
205.850,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
13.4 /
18.4
|
Other elements in 5g0x:
The structure of Pseudomonas Aeruginosa Hdah Bound to Acetate. also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Pseudomonas Aeruginosa Hdah Bound to Acetate.
(pdb code 5g0x). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the
Pseudomonas Aeruginosa Hdah Bound to Acetate., PDB code: 5g0x:
Jump to Potassium binding site number:
1;
2;
3;
4;
Potassium binding site 1 out
of 4 in 5g0x
Go back to
Potassium Binding Sites List in 5g0x
Potassium binding site 1 out
of 4 in the Pseudomonas Aeruginosa Hdah Bound to Acetate.
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Pseudomonas Aeruginosa Hdah Bound to Acetate. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K1373
b:10.6
occ:1.00
|
O
|
A:ASP181
|
2.6
|
9.6
|
1.0
|
O
|
A:LEU203
|
2.6
|
9.7
|
1.0
|
O
|
A:HIS183
|
2.6
|
8.4
|
1.0
|
OD1
|
A:ASP179
|
2.6
|
11.8
|
1.0
|
OG
|
A:SER202
|
2.7
|
10.3
|
1.0
|
O
|
A:ASP179
|
2.7
|
10.6
|
1.0
|
CG
|
A:ASP179
|
3.3
|
11.6
|
1.0
|
C
|
A:ASP179
|
3.5
|
9.8
|
1.0
|
C
|
A:LEU203
|
3.6
|
10.2
|
1.0
|
C
|
A:ASP181
|
3.6
|
9.1
|
1.0
|
C
|
A:HIS183
|
3.7
|
9.3
|
1.0
|
CB
|
A:SER202
|
3.8
|
9.4
|
1.0
|
N
|
A:LEU203
|
3.8
|
11.1
|
1.0
|
CB
|
A:ASP179
|
3.8
|
11.0
|
1.0
|
OD2
|
A:ASP179
|
4.0
|
11.9
|
1.0
|
N
|
A:ASP181
|
4.0
|
8.9
|
1.0
|
CB
|
A:HIS204
|
4.0
|
9.8
|
1.0
|
CA
|
A:SER202
|
4.1
|
9.8
|
1.0
|
N
|
A:GLY185
|
4.1
|
10.0
|
1.0
|
C
|
A:SER202
|
4.2
|
10.8
|
1.0
|
N
|
A:TRP180
|
4.2
|
9.1
|
1.0
|
CA
|
A:ASP179
|
4.3
|
10.9
|
1.0
|
CA
|
A:ASP181
|
4.3
|
9.7
|
1.0
|
C
|
A:TRP180
|
4.3
|
8.9
|
1.0
|
CA
|
A:HIS184
|
4.3
|
9.7
|
1.0
|
CA
|
A:LEU203
|
4.4
|
10.7
|
1.0
|
CA
|
A:TRP180
|
4.4
|
9.1
|
1.0
|
N
|
A:HIS204
|
4.4
|
8.9
|
1.0
|
N
|
A:HIS183
|
4.4
|
8.9
|
1.0
|
CA
|
A:HIS204
|
4.4
|
9.5
|
1.0
|
CB
|
A:ASP181
|
4.4
|
9.6
|
1.0
|
N
|
A:HIS184
|
4.4
|
9.4
|
1.0
|
C
|
A:HIS184
|
4.5
|
9.8
|
1.0
|
O
|
A:HOH2136
|
4.5
|
10.7
|
1.0
|
ND1
|
A:HIS204
|
4.5
|
12.9
|
1.0
|
C
|
A:VAL182
|
4.6
|
9.4
|
1.0
|
N
|
A:VAL182
|
4.7
|
8.3
|
1.0
|
CA
|
A:HIS183
|
4.7
|
8.8
|
1.0
|
CE1
|
A:HIS143
|
4.7
|
11.4
|
1.0
|
CG
|
A:HIS204
|
4.8
|
10.7
|
1.0
|
ND1
|
A:HIS143
|
4.9
|
10.7
|
1.0
|
CA
|
A:VAL182
|
4.9
|
9.3
|
1.0
|
CA
|
A:GLY185
|
5.0
|
10.1
|
1.0
|
|
Potassium binding site 2 out
of 4 in 5g0x
Go back to
Potassium Binding Sites List in 5g0x
Potassium binding site 2 out
of 4 in the Pseudomonas Aeruginosa Hdah Bound to Acetate.
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Pseudomonas Aeruginosa Hdah Bound to Acetate. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K1374
b:11.3
occ:1.00
|
O
|
A:TYR192
|
2.6
|
10.3
|
1.0
|
O
|
A:VAL198
|
2.6
|
11.2
|
1.0
|
O
|
A:HOH2146
|
2.6
|
10.7
|
1.0
|
O
|
A:PHE227
|
2.7
|
11.1
|
1.0
|
O
|
A:ARG195
|
2.8
|
12.8
|
1.0
|
O
|
A:HOH2143
|
2.8
|
12.2
|
1.0
|
C
|
A:PHE227
|
3.5
|
12.3
|
1.0
|
C
|
A:TYR192
|
3.6
|
10.5
|
1.0
|
CB
|
A:PHE227
|
3.7
|
13.9
|
1.0
|
OG
|
A:SER200
|
3.8
|
12.1
|
1.0
|
C
|
A:VAL198
|
3.8
|
11.3
|
1.0
|
CB
|
A:TYR192
|
3.9
|
10.2
|
1.0
|
C
|
A:ARG195
|
3.9
|
12.0
|
1.0
|
CA
|
A:PHE227
|
4.2
|
13.0
|
1.0
|
N
|
A:SER200
|
4.3
|
11.2
|
1.0
|
CA
|
A:TYR192
|
4.3
|
10.1
|
1.0
|
N
|
A:ASN228
|
4.3
|
11.0
|
1.0
|
N
|
A:TYR193
|
4.4
|
10.3
|
1.0
|
N
|
A:ARG195
|
4.5
|
12.4
|
1.0
|
CA
|
A:TYR193
|
4.5
|
10.3
|
1.0
|
CA
|
A:LEU199
|
4.6
|
10.8
|
1.0
|
CA
|
A:ARG195
|
4.6
|
12.5
|
1.0
|
C
|
A:TYR193
|
4.6
|
10.3
|
1.0
|
O
|
A:TYR193
|
4.7
|
11.5
|
1.0
|
N
|
A:LEU199
|
4.7
|
9.5
|
1.0
|
CB
|
A:ASN228
|
4.7
|
11.9
|
1.0
|
CA
|
A:ASN228
|
4.8
|
12.3
|
1.0
|
CB
|
A:ARG195
|
4.8
|
13.3
|
1.0
|
CB
|
A:SER200
|
4.8
|
13.6
|
1.0
|
O
|
A:GLY224
|
4.8
|
12.2
|
1.0
|
CA
|
A:VAL198
|
4.8
|
11.4
|
1.0
|
C
|
A:LEU199
|
4.9
|
11.3
|
1.0
|
CB
|
A:VAL198
|
4.9
|
13.2
|
1.0
|
|
Potassium binding site 3 out
of 4 in 5g0x
Go back to
Potassium Binding Sites List in 5g0x
Potassium binding site 3 out
of 4 in the Pseudomonas Aeruginosa Hdah Bound to Acetate.
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Pseudomonas Aeruginosa Hdah Bound to Acetate. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K1379
b:11.3
occ:1.00
|
O
|
C:VAL198
|
2.6
|
11.1
|
1.0
|
O
|
C:HOH2153
|
2.6
|
11.1
|
1.0
|
O
|
C:TYR192
|
2.6
|
10.1
|
1.0
|
O
|
C:PHE227
|
2.7
|
10.1
|
1.0
|
O
|
C:ARG195
|
2.7
|
13.4
|
1.0
|
O
|
C:HOH2149
|
2.7
|
12.6
|
1.0
|
C
|
C:PHE227
|
3.5
|
10.2
|
1.0
|
C
|
C:TYR192
|
3.6
|
10.6
|
1.0
|
CB
|
C:PHE227
|
3.7
|
10.3
|
1.0
|
CB
|
C:TYR192
|
3.8
|
10.8
|
1.0
|
C
|
C:VAL198
|
3.8
|
11.0
|
1.0
|
OG
|
C:SER200
|
3.9
|
9.4
|
1.0
|
C
|
C:ARG195
|
3.9
|
11.8
|
1.0
|
CA
|
C:PHE227
|
4.2
|
10.3
|
1.0
|
CA
|
C:TYR192
|
4.3
|
10.9
|
1.0
|
N
|
C:SER200
|
4.3
|
10.4
|
1.0
|
N
|
C:ASN228
|
4.4
|
9.9
|
1.0
|
N
|
C:ARG195
|
4.5
|
11.4
|
1.0
|
N
|
C:TYR193
|
4.5
|
9.9
|
1.0
|
CA
|
C:TYR193
|
4.6
|
10.6
|
1.0
|
CA
|
C:ARG195
|
4.6
|
12.0
|
1.0
|
CA
|
C:LEU199
|
4.6
|
11.8
|
1.0
|
N
|
C:LEU199
|
4.7
|
11.7
|
1.0
|
C
|
C:TYR193
|
4.7
|
10.9
|
1.0
|
O
|
C:TYR193
|
4.7
|
11.2
|
1.0
|
CB
|
C:ARG195
|
4.7
|
11.8
|
1.0
|
CB
|
C:ASN228
|
4.7
|
10.3
|
1.0
|
CA
|
C:ASN228
|
4.8
|
10.4
|
1.0
|
CB
|
C:SER200
|
4.8
|
11.0
|
1.0
|
O
|
C:GLY224
|
4.8
|
12.0
|
1.0
|
CA
|
C:VAL198
|
4.8
|
11.1
|
1.0
|
CB
|
C:VAL198
|
4.9
|
11.8
|
1.0
|
C
|
C:LEU199
|
4.9
|
11.0
|
1.0
|
CG
|
C:PHE227
|
4.9
|
10.8
|
1.0
|
|
Potassium binding site 4 out
of 4 in 5g0x
Go back to
Potassium Binding Sites List in 5g0x
Potassium binding site 4 out
of 4 in the Pseudomonas Aeruginosa Hdah Bound to Acetate.
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Pseudomonas Aeruginosa Hdah Bound to Acetate. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K1380
b:10.6
occ:1.00
|
O
|
C:ASP181
|
2.6
|
9.7
|
1.0
|
OD1
|
C:ASP179
|
2.6
|
9.8
|
1.0
|
O
|
C:HIS183
|
2.6
|
8.7
|
1.0
|
O
|
C:LEU203
|
2.6
|
9.2
|
1.0
|
OG
|
C:SER202
|
2.7
|
10.2
|
1.0
|
O
|
C:ASP179
|
2.7
|
9.6
|
1.0
|
CG
|
C:ASP179
|
3.2
|
11.1
|
1.0
|
C
|
C:ASP179
|
3.5
|
9.3
|
1.0
|
C
|
C:LEU203
|
3.6
|
9.2
|
1.0
|
C
|
C:ASP181
|
3.6
|
9.9
|
1.0
|
C
|
C:HIS183
|
3.7
|
9.5
|
1.0
|
CB
|
C:ASP179
|
3.8
|
10.6
|
1.0
|
CB
|
C:SER202
|
3.8
|
9.9
|
1.0
|
N
|
C:LEU203
|
3.9
|
9.5
|
1.0
|
OD2
|
C:ASP179
|
4.0
|
12.1
|
1.0
|
N
|
C:ASP181
|
4.0
|
9.2
|
1.0
|
CB
|
C:HIS204
|
4.1
|
8.7
|
1.0
|
N
|
C:GLY185
|
4.1
|
10.8
|
1.0
|
CA
|
C:SER202
|
4.1
|
9.7
|
1.0
|
N
|
C:TRP180
|
4.2
|
9.6
|
1.0
|
CA
|
C:ASP181
|
4.3
|
9.9
|
1.0
|
CA
|
C:ASP179
|
4.3
|
10.1
|
1.0
|
C
|
C:SER202
|
4.3
|
8.8
|
1.0
|
C
|
C:TRP180
|
4.3
|
9.6
|
1.0
|
CA
|
C:HIS184
|
4.3
|
10.1
|
1.0
|
N
|
C:HIS183
|
4.4
|
8.6
|
1.0
|
CA
|
C:TRP180
|
4.4
|
9.2
|
1.0
|
CB
|
C:ASP181
|
4.4
|
9.8
|
1.0
|
CA
|
C:LEU203
|
4.4
|
9.8
|
1.0
|
N
|
C:HIS204
|
4.4
|
8.7
|
1.0
|
N
|
C:HIS184
|
4.5
|
9.3
|
1.0
|
CA
|
C:HIS204
|
4.5
|
8.9
|
1.0
|
C
|
C:HIS184
|
4.5
|
10.4
|
1.0
|
ND1
|
C:HIS204
|
4.5
|
10.1
|
1.0
|
O
|
C:HOH2143
|
4.6
|
11.4
|
1.0
|
C
|
C:VAL182
|
4.6
|
9.7
|
1.0
|
N
|
C:VAL182
|
4.7
|
9.9
|
1.0
|
CE1
|
C:HIS143
|
4.7
|
12.9
|
1.0
|
CA
|
C:HIS183
|
4.7
|
9.2
|
1.0
|
CG
|
C:HIS204
|
4.8
|
8.9
|
1.0
|
ND1
|
C:HIS143
|
4.9
|
12.5
|
1.0
|
CA
|
C:VAL182
|
4.9
|
10.3
|
1.0
|
CA
|
C:GLY185
|
4.9
|
11.2
|
1.0
|
|
Reference:
A.Kramer,
T.Wagner,
O.Yildiz,
F.J.Meyer-Almes.
Crystal Structure of A Histone Deacetylase Homologue From Pseudomonas Aeruginosa. Biochemistry V. 55 6858 2016.
ISSN: ISSN 1520-4995
PubMed: 27951649
DOI: 10.1021/ACS.BIOCHEM.6B00613
Page generated: Mon Aug 12 13:41:39 2024
|