Sodium in PDB 8a1w: Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q1
Enzymatic activity of Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q1
All present enzymatic activity of Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q1:
7.2.1.1;
Other elements in 8a1w:
The structure of Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q1 also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q1
(pdb code 8a1w). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the
Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q1, PDB code: 8a1w:
Jump to Sodium binding site number:
1;
2;
Sodium binding site 1 out
of 2 in 8a1w
Go back to
Sodium Binding Sites List in 8a1w
Sodium binding site 1 out
of 2 in the Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q1
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 1 of Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na509
b:22.2
occ:1.00
|
O
|
B:VAL275
|
2.3
|
14.9
|
1.0
|
O
|
B:VAL332
|
2.3
|
12.3
|
1.0
|
O
|
B:ALA263
|
2.4
|
12.1
|
1.0
|
O
|
B:HOH692
|
2.5
|
12.2
|
1.0
|
HD11
|
B:ILE268
|
2.9
|
13.1
|
1.0
|
O
|
B:HOH602
|
3.1
|
13.8
|
1.0
|
C
|
B:VAL332
|
3.3
|
1.4
|
1.0
|
C
|
B:ALA263
|
3.3
|
9.2
|
1.0
|
C
|
B:VAL275
|
3.4
|
11.1
|
1.0
|
HB1
|
B:ALA263
|
3.4
|
11.2
|
1.0
|
HB
|
B:VAL332
|
3.4
|
10.9
|
1.0
|
H
|
B:THR277
|
3.6
|
11.7
|
1.0
|
HA
|
B:VAL332
|
3.6
|
11.0
|
1.0
|
HA
|
B:VAL275
|
3.6
|
11.8
|
1.0
|
OG1
|
B:THR277
|
3.7
|
15.9
|
1.0
|
CD1
|
B:ILE268
|
3.7
|
12.4
|
1.0
|
HA
|
B:ALA263
|
3.7
|
12.3
|
1.0
|
HD13
|
B:ILE268
|
3.7
|
13.0
|
1.0
|
HA2
|
B:GLY266
|
3.8
|
12.2
|
1.0
|
CA
|
B:VAL332
|
3.9
|
7.0
|
1.0
|
CA
|
B:ALA263
|
4.0
|
8.9
|
1.0
|
HA
|
B:LEU333
|
4.0
|
9.5
|
1.0
|
HG1
|
B:THR277
|
4.1
|
12.1
|
1.0
|
CA
|
B:VAL275
|
4.1
|
14.1
|
1.0
|
HA
|
B:PHE264
|
4.1
|
11.8
|
1.0
|
CB
|
B:VAL332
|
4.1
|
10.1
|
1.0
|
CB
|
B:ALA263
|
4.2
|
8.0
|
1.0
|
N
|
B:THR277
|
4.2
|
15.6
|
1.0
|
N
|
B:LEU333
|
4.2
|
9.2
|
1.0
|
HG12
|
B:ILE268
|
4.3
|
13.0
|
1.0
|
O
|
B:GLU274
|
4.3
|
16.5
|
1.0
|
HA
|
B:SER276
|
4.3
|
11.5
|
1.0
|
HD12
|
B:ILE268
|
4.3
|
13.7
|
1.0
|
N
|
B:PHE264
|
4.3
|
7.5
|
1.0
|
N
|
B:SER276
|
4.5
|
11.0
|
1.0
|
HB
|
B:THR277
|
4.5
|
11.4
|
1.0
|
H
|
B:GLY266
|
4.5
|
12.3
|
1.0
|
CG1
|
B:ILE268
|
4.5
|
12.7
|
1.0
|
O
|
B:HOH618
|
4.5
|
4.3
|
1.0
|
HD23
|
B:LEU333
|
4.6
|
8.8
|
1.0
|
CB
|
B:THR277
|
4.6
|
11.6
|
1.0
|
CA
|
B:LEU333
|
4.6
|
4.7
|
1.0
|
CA
|
B:PHE264
|
4.6
|
7.0
|
1.0
|
HG23
|
B:VAL332
|
4.7
|
9.7
|
1.0
|
CA
|
B:GLY266
|
4.7
|
11.6
|
1.0
|
HB3
|
B:ALA263
|
4.7
|
11.6
|
1.0
|
HG13
|
B:ILE268
|
4.7
|
13.2
|
1.0
|
HB
|
B:VAL275
|
4.7
|
11.6
|
1.0
|
CA
|
B:SER276
|
4.7
|
7.6
|
1.0
|
O
|
B:PHE264
|
4.8
|
8.7
|
1.0
|
N
|
B:GLY266
|
4.8
|
9.2
|
1.0
|
C
|
B:SER276
|
4.8
|
12.6
|
1.0
|
HB2
|
B:ALA263
|
4.8
|
11.6
|
1.0
|
C
|
B:PHE264
|
4.8
|
8.6
|
1.0
|
CA
|
B:THR277
|
4.9
|
7.4
|
1.0
|
H
|
B:LEU333
|
5.0
|
10.0
|
1.0
|
|
Sodium binding site 2 out
of 2 in 8a1w
Go back to
Sodium Binding Sites List in 8a1w
Sodium binding site 2 out
of 2 in the Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q1
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 2 of Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na510
b:21.1
occ:1.00
|
O
|
B:TYR378
|
2.4
|
18.7
|
1.0
|
O
|
B:ASN375
|
2.4
|
17.2
|
1.0
|
O
|
B:HOH695
|
2.4
|
20.3
|
1.0
|
O
|
B:ILE371
|
2.5
|
13.6
|
1.0
|
O
|
B:ARG372
|
2.5
|
0.1
|
1.0
|
HA
|
B:ARG372
|
2.9
|
10.0
|
1.0
|
C
|
B:ARG372
|
3.1
|
3.7
|
1.0
|
HA
|
B:PRO379
|
3.3
|
13.7
|
1.0
|
H
|
B:ASN375
|
3.3
|
10.9
|
1.0
|
C
|
B:ASN375
|
3.4
|
11.8
|
1.0
|
CA
|
B:ARG372
|
3.4
|
8.5
|
1.0
|
HB3
|
B:ASN375
|
3.5
|
12.3
|
1.0
|
C
|
B:TYR378
|
3.5
|
12.1
|
1.0
|
C
|
B:ILE371
|
3.6
|
6.4
|
1.0
|
O
|
B:HOH622
|
3.7
|
16.6
|
1.0
|
O
|
B:HOH609
|
3.8
|
17.3
|
1.0
|
N
|
B:ASN375
|
4.0
|
9.5
|
1.0
|
CA
|
B:PRO379
|
4.0
|
12.6
|
1.0
|
N
|
B:ARG372
|
4.0
|
13.8
|
1.0
|
N
|
B:VAL373
|
4.0
|
3.8
|
1.0
|
H
|
B:TYR378
|
4.0
|
11.4
|
1.0
|
CA
|
B:ASN375
|
4.1
|
10.6
|
1.0
|
O
|
B:HOH681
|
4.1
|
11.8
|
1.0
|
O
|
B:PRO379
|
4.1
|
13.8
|
1.0
|
C
|
B:PRO379
|
4.2
|
9.3
|
1.0
|
N
|
B:PRO379
|
4.2
|
14.0
|
1.0
|
HA
|
B:PRO376
|
4.2
|
12.1
|
1.0
|
CB
|
B:ASN375
|
4.2
|
12.0
|
1.0
|
HG22
|
B:ILE371
|
4.4
|
10.8
|
1.0
|
N
|
B:PRO376
|
4.4
|
16.0
|
1.0
|
N
|
B:TYR378
|
4.5
|
10.9
|
1.0
|
HB2
|
B:TYR378
|
4.5
|
12.3
|
1.0
|
C
|
B:VAL373
|
4.5
|
6.4
|
1.0
|
CA
|
B:TYR378
|
4.5
|
10.1
|
1.0
|
H
|
B:VAL373
|
4.6
|
9.4
|
1.0
|
CA
|
B:PRO376
|
4.6
|
11.2
|
1.0
|
HG3
|
B:MET322
|
4.6
|
11.3
|
1.0
|
HA
|
B:VAL373
|
4.6
|
10.2
|
1.0
|
O
|
B:VAL373
|
4.6
|
16.6
|
1.0
|
CA
|
B:VAL373
|
4.7
|
4.9
|
1.0
|
C
|
B:PRO376
|
4.7
|
8.2
|
1.0
|
O
|
B:PRO376
|
4.7
|
15.4
|
1.0
|
HG23
|
B:ILE371
|
4.8
|
11.0
|
1.0
|
CB
|
B:ARG372
|
4.8
|
1.8
|
1.0
|
N
|
B:VAL374
|
4.8
|
7.9
|
1.0
|
H
|
B:ARG372
|
4.8
|
10.9
|
1.0
|
HB2
|
B:ASN375
|
4.9
|
10.3
|
1.0
|
H
|
B:VAL374
|
4.9
|
9.1
|
1.0
|
HB3
|
B:ARG372
|
4.9
|
9.1
|
1.0
|
CA
|
B:ILE371
|
4.9
|
5.7
|
1.0
|
HE2
|
B:MET322
|
4.9
|
11.1
|
1.0
|
HA
|
B:ILE371
|
4.9
|
11.3
|
1.0
|
N
|
B:GLU380
|
5.0
|
12.2
|
1.0
|
O
|
B:HOH713
|
5.0
|
24.6
|
1.0
|
|
Reference:
J.-L.Hau,
J.-L.Hau,
S.Kaltwasser,
J.Vonck,
G.Fritz,
J.Steuber.
N/A N/A.
Page generated: Wed Oct 9 10:25:34 2024
|