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Crystal structure of human AQP10

Analyse Crystal structure of human AQP10 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6F7H
Type: protein
Length: 1,012 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aquaporin-10
UniProt: Q96PS8
Ligands: BNG
Pockets: 15 · best druggability 0.87

Structure

x-ray diffraction · 4 distinct chains · 71% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aquaporin-10	protein	251	73% helix, 0% strand	Q96PS8
B	Aquaporin-10	protein	252	71% helix, 0% strand	Q96PS8
C	Aquaporin-10	protein	253	72% helix, 0% strand	Q96PS8
D	Aquaporin-10	protein	256	70% helix, 0% strand	Q96PS8

Ligands and binding sites

BNG · nonyl beta-D-glucopyranoside · ligand · 16 copies · chains A, B, D, C
GOL · Glycerol · additive · 6 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	749	0.87	0.90	51	GOL
2	499	0.78	0.85	64	GOL
3	528	0.77	0.84	60	GOL
4	505	0.77	0.84	58	GOL
5	517	0.77	0.84	54	GOL

Interfaces

5 interfaces between chains.

A–D · 1483 Å² buried · 16 hydrogen bonds · protein-protein
B–C · 1397 Å² buried · 16 hydrogen bonds · protein-protein
C–D · 1335 Å² buried · 14 hydrogen bonds · protein-protein
A–B · 1280 Å² buried · 14 hydrogen bonds · protein-protein
B–D · 18 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

6F7H · Crystal structure of human AQP10 · the same entry in another collection · chain D against D, TM-score 1.00
Q96PS8 · AlphaFold monomer V2.0 prediction for aquaporin-10 (Q96PS8) · a predicted model of the same protein · chain D against A, TM-score 0.97

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q96PS8
Elsewhere: RCSB PDB 6F7H · PDBe 6F7H · UniProt Q96PS8

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