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Crystal structure of the S156E mutant of human aquaporin 5

Analyse Crystal structure of the S156E mutant of human aquaporin 5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5C5X
Type: protein
Length: 1,952 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aquaporin-5
UniProt: P55064
Ligands: PS6
Pockets: 20 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 70% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H	Aquaporin-5	protein	244	70% helix, 0% strand	P55064

Ligands and binding sites

PS6 · O-[(S)-{[(2S)-2-(hexanoyloxy)-3-(tetradecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-D-serine · ligand · 2 copies · chains A, B, C, D, E, F, G, H

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

Pockets

20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	252	0.81	0.92	39	PS6
2	246	0.80	0.91	36	PS6
3	696	0.70	0.77	87	empty
4	744	0.70	0.77	87	empty
5	617	0.69	0.78	71	empty

Interfaces

20 interfaces between chains.

B–C · 1596 Å² buried · 10 hydrogen bonds · protein-protein
A–C · 1594 Å² buried · 9 hydrogen bonds · protein-protein
A–D · 1593 Å² buried · 12 hydrogen bonds · protein-protein
F–G · 1590 Å² buried · 9 hydrogen bonds · protein-protein
B–D · 1586 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

5C5X · Crystal structure of the S156E mutant of human aquaporin 5 · the same entry in another collection · chain H against H, TM-score 1.00
P55064 · AlphaFold monomer V2.0 prediction for aquaporin-5 (P55064) · a predicted model of the same protein · chain C against A, TM-score 1.00

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 P55064
Elsewhere: RCSB PDB 5C5X · PDBe 5C5X · UniProt P55064

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