Sodium in PDB 8fht: Cryo-Em Structure of Human Ncc
Other elements in 8fht:
The structure of Cryo-Em Structure of Human Ncc also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Cryo-Em Structure of Human Ncc
(pdb code 8fht). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the
Cryo-Em Structure of Human Ncc, PDB code: 8fht:
Jump to Sodium binding site number:
1;
2;
Sodium binding site 1 out
of 2 in 8fht
Go back to
Sodium Binding Sites List in 8fht
Sodium binding site 1 out
of 2 in the Cryo-Em Structure of Human Ncc
 Mono view
 Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 1 of Cryo-Em Structure of Human Ncc within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na1101
b:31.8
occ:1.00
|
O
|
A:TRP151
|
2.2
|
27.9
|
1.0
|
OG
|
A:SER468
|
2.3
|
33.8
|
1.0
|
O
|
A:LEU148
|
2.3
|
34.6
|
1.0
|
O
|
A:ALA464
|
2.5
|
33.1
|
1.0
|
OG
|
A:SER467
|
2.7
|
35.2
|
1.0
|
C
|
A:ALA464
|
3.2
|
33.1
|
1.0
|
CA
|
A:ALA464
|
3.3
|
33.1
|
1.0
|
N
|
A:SER468
|
3.4
|
33.8
|
1.0
|
C
|
A:TRP151
|
3.5
|
27.9
|
1.0
|
C
|
A:LEU148
|
3.6
|
34.6
|
1.0
|
CB
|
A:SER468
|
3.6
|
33.8
|
1.0
|
CB
|
A:SER467
|
3.8
|
35.2
|
1.0
|
CB
|
A:ALA464
|
3.8
|
33.1
|
1.0
|
CA
|
A:SER468
|
3.9
|
33.8
|
1.0
|
CA
|
A:GLY152
|
4.2
|
26.1
|
1.0
|
C
|
A:SER467
|
4.2
|
35.2
|
1.0
|
N
|
A:GLY152
|
4.3
|
26.1
|
1.0
|
CA
|
A:LEU148
|
4.4
|
34.6
|
1.0
|
CA
|
A:TRP151
|
4.5
|
27.9
|
1.0
|
N
|
A:THR465
|
4.5
|
33.4
|
1.0
|
CA
|
A:SER467
|
4.5
|
35.2
|
1.0
|
N
|
A:ASN149
|
4.5
|
31.1
|
1.0
|
O
|
A:GLY463
|
4.5
|
34.4
|
1.0
|
CA
|
A:ASN149
|
4.5
|
31.1
|
1.0
|
O
|
A:ASN149
|
4.6
|
31.1
|
1.0
|
CD2
|
A:LEU148
|
4.6
|
34.6
|
1.0
|
N
|
A:ALA464
|
4.6
|
33.1
|
1.0
|
CB
|
A:TRP151
|
4.7
|
27.9
|
1.0
|
C
|
A:ASN149
|
4.7
|
31.1
|
1.0
|
N
|
A:TRP151
|
4.7
|
27.9
|
1.0
|
N
|
A:SER467
|
4.8
|
35.2
|
1.0
|
CB
|
A:LEU148
|
4.9
|
34.6
|
1.0
|
|
Sodium binding site 2 out
of 2 in 8fht
Go back to
Sodium Binding Sites List in 8fht
Sodium binding site 2 out
of 2 in the Cryo-Em Structure of Human Ncc
 Mono view
 Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 2 of Cryo-Em Structure of Human Ncc within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na1101
b:31.6
occ:1.00
|
O
|
B:TRP151
|
2.2
|
28.1
|
1.0
|
OG
|
B:SER468
|
2.3
|
33.9
|
1.0
|
O
|
B:LEU148
|
2.4
|
34.4
|
1.0
|
O
|
B:ALA464
|
2.4
|
33.2
|
1.0
|
OG
|
B:SER467
|
2.7
|
35.4
|
1.0
|
C
|
B:ALA464
|
3.2
|
33.2
|
1.0
|
CA
|
B:ALA464
|
3.3
|
33.2
|
1.0
|
N
|
B:SER468
|
3.4
|
33.9
|
1.0
|
C
|
B:TRP151
|
3.5
|
28.1
|
1.0
|
CB
|
B:SER468
|
3.6
|
33.9
|
1.0
|
C
|
B:LEU148
|
3.6
|
34.4
|
1.0
|
CB
|
B:ALA464
|
3.8
|
33.2
|
1.0
|
CB
|
B:SER467
|
3.8
|
35.4
|
1.0
|
CA
|
B:SER468
|
3.9
|
33.9
|
1.0
|
CA
|
B:GLY152
|
4.2
|
26.0
|
1.0
|
C
|
B:SER467
|
4.2
|
35.4
|
1.0
|
N
|
B:GLY152
|
4.3
|
26.0
|
1.0
|
CA
|
B:LEU148
|
4.4
|
34.4
|
1.0
|
N
|
B:THR465
|
4.4
|
33.4
|
1.0
|
CA
|
B:SER467
|
4.5
|
35.4
|
1.0
|
CA
|
B:TRP151
|
4.5
|
28.1
|
1.0
|
O
|
B:GLY463
|
4.5
|
34.8
|
1.0
|
N
|
B:ASN149
|
4.5
|
31.3
|
1.0
|
O
|
B:ASN149
|
4.6
|
31.3
|
1.0
|
CA
|
B:ASN149
|
4.6
|
31.3
|
1.0
|
N
|
B:ALA464
|
4.6
|
33.2
|
1.0
|
CD2
|
B:LEU148
|
4.6
|
34.4
|
1.0
|
CB
|
B:TRP151
|
4.7
|
28.1
|
1.0
|
C
|
B:ASN149
|
4.7
|
31.3
|
1.0
|
N
|
B:TRP151
|
4.7
|
28.1
|
1.0
|
N
|
B:SER467
|
4.7
|
35.4
|
1.0
|
CB
|
B:LEU148
|
4.9
|
34.4
|
1.0
|
|
Reference:
M.Fan,
J.Zhang,
C.Lee,
J.Zhang,
L.Feng.
Structure and Thiazide Inhibition Mechanism of the Human Na-Cl Cotransporter Nature 2023.
ISSN: ESSN 1476-4687
DOI: 10.1038/S41586-023-05718-0
Page generated: Wed Oct 9 11:53:30 2024
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