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ATPase crystal structure with bound phosphate analogue

Analyse ATPase crystal structure with bound phosphate analogue in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BEV
Type: protein
Length: 663 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Copper efflux ATPase
EC: 3.6.3.-
UniProt: Q5ZWR1
Ligands: MGF, MG
Pockets: 9 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Copper efflux ATPase (EC 3.6.3.-)	protein	663	49% helix, 14% strand	Q5ZWR1

Ligands and binding sites

MGF · Trifluoromagnesate · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	614	0.70	0.78	77	empty
2	386	0.63	0.78	57	empty
3	139	0.41	0.75	22	empty
4	50	0.38	0.81	15	empty
5	64	0.30	0.74	13	empty

Compared structures

4BEV · ATPase crystal structure with bound phosphate analogue · the same entry in another collection · chain A against A, TM-score 1.00
Q5ZWR1 · AlphaFold monomer V2.0 prediction for copper-exporting P-type ATPase (Q5ZWR1) · a predicted model of the same protein · chain A against A, TM-score 0.73

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 Q5ZWR1
Elsewhere: RCSB PDB 4BEV · PDBe 4BEV · UniProt Q5ZWR1

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