Potassium in PDB 5g11: Pseudomonas Aeruginosa Hdah Bound to Pfsaha.
Protein crystallography data
The structure of Pseudomonas Aeruginosa Hdah Bound to Pfsaha., PDB code: 5g11
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)
|
75.96 /
2.48
|
Space group
|
P 41 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
81.790,
81.790,
204.860,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
16.8 /
22.4
|
Other elements in 5g11:
The structure of Pseudomonas Aeruginosa Hdah Bound to Pfsaha. also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Pseudomonas Aeruginosa Hdah Bound to Pfsaha.
(pdb code 5g11). 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 Pfsaha., PDB code: 5g11:
Jump to Potassium binding site number:
1;
2;
3;
4;
Potassium binding site 1 out
of 4 in 5g11
Go back to
Potassium Binding Sites List in 5g11
Potassium binding site 1 out
of 4 in the Pseudomonas Aeruginosa Hdah Bound to Pfsaha.
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 Pfsaha. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K1374
b:12.1
occ:1.00
|
O
|
A:ASP181
|
2.6
|
11.9
|
1.0
|
O
|
A:LEU203
|
2.6
|
12.8
|
1.0
|
O
|
A:HIS183
|
2.6
|
12.1
|
1.0
|
OD1
|
A:ASP179
|
2.6
|
11.6
|
1.0
|
OG
|
A:SER202
|
2.6
|
12.0
|
1.0
|
O
|
A:ASP179
|
2.6
|
11.5
|
1.0
|
CG
|
A:ASP179
|
3.2
|
11.5
|
1.0
|
C
|
A:ASP179
|
3.4
|
11.3
|
1.0
|
C
|
A:LEU203
|
3.6
|
12.9
|
1.0
|
C
|
A:ASP181
|
3.7
|
12.1
|
1.0
|
C
|
A:HIS183
|
3.7
|
12.2
|
1.0
|
CB
|
A:ASP179
|
3.8
|
11.5
|
1.0
|
CB
|
A:SER202
|
3.9
|
11.9
|
1.0
|
N
|
A:LEU203
|
3.9
|
12.4
|
1.0
|
OD2
|
A:ASP179
|
3.9
|
11.6
|
1.0
|
N
|
A:ASP181
|
4.0
|
12.0
|
1.0
|
CB
|
A:HIS204
|
4.1
|
13.4
|
1.0
|
CA
|
A:SER202
|
4.1
|
11.8
|
1.0
|
N
|
A:GLY185
|
4.1
|
12.3
|
1.0
|
N
|
A:TRP180
|
4.2
|
11.2
|
1.0
|
CA
|
A:ASP179
|
4.2
|
11.4
|
1.0
|
C
|
A:SER202
|
4.3
|
12.1
|
1.0
|
CA
|
A:ASP181
|
4.3
|
12.4
|
1.0
|
CA
|
A:TRP180
|
4.3
|
11.2
|
1.0
|
C
|
A:TRP180
|
4.3
|
11.6
|
1.0
|
CA
|
A:HIS184
|
4.4
|
12.0
|
1.0
|
CA
|
A:LEU203
|
4.4
|
12.8
|
1.0
|
N
|
A:HIS204
|
4.4
|
12.9
|
1.0
|
CB
|
A:ASP181
|
4.4
|
12.8
|
1.0
|
CA
|
A:HIS204
|
4.5
|
13.1
|
1.0
|
N
|
A:HIS184
|
4.5
|
12.0
|
1.0
|
N
|
A:HIS183
|
4.5
|
12.1
|
1.0
|
O
|
A:HOH2066
|
4.5
|
10.2
|
1.0
|
C
|
A:HIS184
|
4.6
|
12.2
|
1.0
|
ND1
|
A:HIS204
|
4.6
|
13.7
|
1.0
|
C
|
A:VAL182
|
4.7
|
11.9
|
1.0
|
N
|
A:VAL182
|
4.7
|
12.0
|
1.0
|
CA
|
A:HIS183
|
4.8
|
12.2
|
1.0
|
CE1
|
A:HIS143
|
4.8
|
12.8
|
1.0
|
CG
|
A:HIS204
|
4.8
|
13.6
|
1.0
|
OD1
|
A:ASP181
|
5.0
|
13.9
|
1.0
|
ND1
|
A:HIS143
|
5.0
|
12.8
|
1.0
|
CA
|
A:GLY185
|
5.0
|
12.2
|
1.0
|
|
Potassium binding site 2 out
of 4 in 5g11
Go back to
Potassium Binding Sites List in 5g11
Potassium binding site 2 out
of 4 in the Pseudomonas Aeruginosa Hdah Bound to Pfsaha.
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 Pfsaha. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K1375
b:11.1
occ:1.00
|
O
|
A:VAL198
|
2.6
|
11.6
|
1.0
|
O
|
A:TYR192
|
2.6
|
10.9
|
1.0
|
O
|
A:HOH2074
|
2.6
|
10.7
|
1.0
|
O
|
A:PHE227
|
2.6
|
11.2
|
1.0
|
O
|
A:HOH2071
|
2.6
|
11.3
|
1.0
|
O
|
A:ARG195
|
2.7
|
12.0
|
1.0
|
C
|
A:PHE227
|
3.5
|
11.6
|
1.0
|
C
|
A:TYR192
|
3.6
|
11.2
|
1.0
|
CB
|
A:PHE227
|
3.8
|
11.6
|
1.0
|
OG
|
A:SER200
|
3.8
|
10.6
|
1.0
|
C
|
A:VAL198
|
3.8
|
11.6
|
1.0
|
C
|
A:ARG195
|
3.8
|
12.7
|
1.0
|
CB
|
A:TYR192
|
3.9
|
11.1
|
1.0
|
CA
|
A:PHE227
|
4.2
|
11.7
|
1.0
|
N
|
A:ASN228
|
4.3
|
11.8
|
1.0
|
CA
|
A:TYR192
|
4.3
|
11.0
|
1.0
|
N
|
A:SER200
|
4.4
|
10.9
|
1.0
|
N
|
A:ARG195
|
4.4
|
12.5
|
1.0
|
N
|
A:TYR193
|
4.5
|
11.3
|
1.0
|
CA
|
A:ARG195
|
4.5
|
12.7
|
1.0
|
CA
|
A:TYR193
|
4.5
|
11.6
|
1.0
|
CA
|
A:LEU199
|
4.6
|
11.1
|
1.0
|
CB
|
A:ARG195
|
4.6
|
13.0
|
1.0
|
CB
|
A:ASN228
|
4.6
|
12.0
|
1.0
|
C
|
A:TYR193
|
4.6
|
11.9
|
1.0
|
N
|
A:LEU199
|
4.6
|
11.3
|
1.0
|
O
|
A:TYR193
|
4.7
|
11.9
|
1.0
|
CA
|
A:ASN228
|
4.7
|
11.9
|
1.0
|
CB
|
A:SER200
|
4.8
|
10.8
|
1.0
|
O
|
A:GLY224
|
4.8
|
14.2
|
1.0
|
CA
|
A:VAL198
|
4.8
|
11.9
|
1.0
|
CB
|
A:VAL198
|
4.9
|
12.1
|
1.0
|
C
|
A:LEU199
|
4.9
|
11.1
|
1.0
|
N
|
A:ASP196
|
4.9
|
12.9
|
1.0
|
|
Potassium binding site 3 out
of 4 in 5g11
Go back to
Potassium Binding Sites List in 5g11
Potassium binding site 3 out
of 4 in the Pseudomonas Aeruginosa Hdah Bound to Pfsaha.
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 Pfsaha. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K1380
b:10.9
occ:1.00
|
O
|
B:TYR192
|
2.6
|
11.5
|
1.0
|
O
|
B:VAL198
|
2.6
|
11.7
|
1.0
|
O
|
B:HOH2079
|
2.6
|
10.2
|
1.0
|
O
|
B:HOH2074
|
2.6
|
10.8
|
1.0
|
O
|
B:PHE227
|
2.6
|
11.1
|
1.0
|
O
|
B:ARG195
|
2.7
|
12.4
|
1.0
|
C
|
B:PHE227
|
3.5
|
11.4
|
1.0
|
C
|
B:TYR192
|
3.5
|
12.0
|
1.0
|
CB
|
B:PHE227
|
3.8
|
11.6
|
1.0
|
C
|
B:VAL198
|
3.8
|
12.0
|
1.0
|
C
|
B:ARG195
|
3.9
|
12.9
|
1.0
|
CB
|
B:TYR192
|
3.9
|
12.5
|
1.0
|
OG
|
B:SER200
|
3.9
|
11.7
|
1.0
|
CA
|
B:PHE227
|
4.2
|
11.7
|
1.0
|
CA
|
B:TYR192
|
4.3
|
12.2
|
1.0
|
N
|
B:ASN228
|
4.3
|
11.3
|
1.0
|
N
|
B:SER200
|
4.4
|
12.0
|
1.0
|
N
|
B:TYR193
|
4.4
|
12.0
|
1.0
|
N
|
B:ARG195
|
4.4
|
13.0
|
1.0
|
CA
|
B:TYR193
|
4.5
|
12.1
|
1.0
|
O
|
B:TYR193
|
4.5
|
12.3
|
1.0
|
CA
|
B:ARG195
|
4.5
|
13.2
|
1.0
|
C
|
B:TYR193
|
4.6
|
12.2
|
1.0
|
CA
|
B:LEU199
|
4.6
|
11.9
|
1.0
|
CB
|
B:ARG195
|
4.6
|
13.7
|
1.0
|
CB
|
B:ASN228
|
4.6
|
11.1
|
1.0
|
N
|
B:LEU199
|
4.6
|
12.0
|
1.0
|
CA
|
B:ASN228
|
4.7
|
11.2
|
1.0
|
CA
|
B:VAL198
|
4.8
|
12.2
|
1.0
|
O
|
B:GLY224
|
4.8
|
13.7
|
1.0
|
CB
|
B:SER200
|
4.8
|
11.9
|
1.0
|
CB
|
B:VAL198
|
4.9
|
12.3
|
1.0
|
C
|
B:LEU199
|
4.9
|
11.9
|
1.0
|
N
|
B:ASP196
|
4.9
|
13.0
|
1.0
|
|
Potassium binding site 4 out
of 4 in 5g11
Go back to
Potassium Binding Sites List in 5g11
Potassium binding site 4 out
of 4 in the Pseudomonas Aeruginosa Hdah Bound to Pfsaha.
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 Pfsaha. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K1381
b:13.3
occ:1.00
|
O
|
B:ASP181
|
2.6
|
12.7
|
1.0
|
OD1
|
B:ASP179
|
2.6
|
13.1
|
1.0
|
O
|
B:HIS183
|
2.6
|
13.2
|
1.0
|
O
|
B:LEU203
|
2.6
|
13.2
|
1.0
|
OG
|
B:SER202
|
2.6
|
13.3
|
1.0
|
O
|
B:ASP179
|
2.6
|
12.6
|
1.0
|
CG
|
B:ASP179
|
3.2
|
13.2
|
1.0
|
C
|
B:ASP179
|
3.4
|
12.6
|
1.0
|
C
|
B:LEU203
|
3.6
|
13.2
|
1.0
|
C
|
B:ASP181
|
3.7
|
12.4
|
1.0
|
C
|
B:HIS183
|
3.7
|
13.1
|
1.0
|
CB
|
B:ASP179
|
3.8
|
13.0
|
1.0
|
CB
|
B:SER202
|
3.9
|
13.3
|
1.0
|
N
|
B:LEU203
|
3.9
|
13.2
|
1.0
|
OD2
|
B:ASP179
|
3.9
|
13.4
|
1.0
|
N
|
B:ASP181
|
4.0
|
12.5
|
1.0
|
CB
|
B:HIS204
|
4.1
|
13.4
|
1.0
|
N
|
B:GLY185
|
4.1
|
12.7
|
1.0
|
CA
|
B:SER202
|
4.1
|
13.1
|
1.0
|
N
|
B:TRP180
|
4.2
|
12.5
|
1.0
|
CA
|
B:ASP179
|
4.2
|
12.7
|
1.0
|
CA
|
B:ASP181
|
4.3
|
12.6
|
1.0
|
C
|
B:SER202
|
4.3
|
13.1
|
1.0
|
CA
|
B:HIS184
|
4.3
|
12.6
|
1.0
|
C
|
B:TRP180
|
4.3
|
12.4
|
1.0
|
CA
|
B:TRP180
|
4.4
|
12.4
|
1.0
|
CB
|
B:ASP181
|
4.4
|
12.8
|
1.0
|
CA
|
B:LEU203
|
4.4
|
13.3
|
1.0
|
N
|
B:HIS204
|
4.4
|
13.2
|
1.0
|
N
|
B:HIS184
|
4.4
|
12.8
|
1.0
|
CA
|
B:HIS204
|
4.5
|
13.5
|
1.0
|
N
|
B:HIS183
|
4.5
|
12.9
|
1.0
|
C
|
B:HIS184
|
4.6
|
12.8
|
1.0
|
O
|
B:HOH2067
|
4.6
|
10.3
|
1.0
|
ND1
|
B:HIS204
|
4.6
|
13.9
|
1.0
|
C
|
B:VAL182
|
4.7
|
12.4
|
1.0
|
CE1
|
B:HIS143
|
4.7
|
13.8
|
1.0
|
N
|
B:VAL182
|
4.7
|
12.3
|
1.0
|
CA
|
B:HIS183
|
4.7
|
13.3
|
1.0
|
CG
|
B:HIS204
|
4.8
|
13.7
|
1.0
|
ND1
|
B:HIS143
|
4.9
|
13.7
|
1.0
|
CA
|
B:GLY185
|
4.9
|
12.7
|
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 13:43:18 2024
|