MolNFT v1 · #172679 · protein

Human TRPV4 structure in presence of 4A-pdd

7AA5 · Transient receptor potential cation channel subfamily V…: “Human TRPV4 structure in presence of 4A-pdd”. Electron microscopy, 1 ligand (CA), 20 pockets (best druggability 0.80). MolNFT v1 #172679 on GenesisL1: 3D structure, binding…

PDB: 7AA5
Type: protein
Length: 2,448 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transient receptor potential cation channel subfamily V member 4,GREEN fluorescent protein
UniProt: Q9HBA0
Ligands: CA
Pockets: 20 · best druggability 0.80

Structure

electron microscopy · 1 distinct chain · 52% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Transient receptor potential cation channel subfamily V member 4,GREEN fluorescent protein	protein	612	52% helix, 3% strand	Q9HBA0

Ligands and binding sites

CA · Calcium ion · metal

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

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	916	0.80	0.81	92	empty
2	1139	0.78	0.79	103	empty
3	489	0.74	0.82	64	empty
4	302	0.74	0.86	50	empty
5	248	0.73	0.87	52	empty

Interfaces

4 interfaces between chains.

B–D · 2075 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 2071 Å² buried · 11 hydrogen bonds · protein-protein
C–D · 2049 Å² buried · 11 hydrogen bonds · protein-protein
A–B · 2014 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

7AA5 · Human TRPV4 structure in presence of 4a-PDD · the same entry in another collection · chain D against D, TM-score 1.00
Q9HBA0 · AlphaFold monomer V2.0 prediction for transient receptor potential cation channel… · a predicted model of the same protein · chain B against A, TM-score 0.92

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 Q9HBA0
Elsewhere: RCSB PDB 7AA5 · PDBe 7AA5 · UniProt Q9HBA0

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