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Xenopus tropicalis TRPV4

Analyse Xenopus tropicalis TRPV4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6BBJ
Type: protein
Length: 2,432 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transient receptor potential cation channel, subfamily V, member 4
UniProt: F7BWY7
Pockets: 20 · best druggability 0.82

Structure

electron microscopy · 1 distinct chain · 55% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Transient receptor potential cation channel, subfamily V, member 4	protein	608	55% helix, 4% strand	F7BWY7

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	995	0.82	0.83	79	empty
2	1081	0.82	0.83	80	empty
3	1081	0.81	0.82	89	empty
4	751	0.76	0.81	53	empty
5	95	0.72	0.94	14	empty

Interfaces

5 interfaces between chains.

A–C · 2316 Å² buried · 3 hydrogen bonds · protein-protein
C–D · 2300 Å² buried · 3 hydrogen bonds · protein-protein
B–D · 2297 Å² buried · 3 hydrogen bonds · protein-protein
A–B · 2285 Å² buried · 3 hydrogen bonds · protein-protein
A–D · 11 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6BBJ · Xenopus Tropicalis TRPV4 · the same entry in another collection · chain A 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 F7BWY7
Elsewhere: RCSB PDB 6BBJ · PDBe 6BBJ · UniProt F7BWY7

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