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Crystal structure of ADP compounds hydrolase

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

PDB: 1VHG
Type: protein
Length: 370 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ADP compounds hydrolase nude
EC: 3.6.1.-
UniProt: P45799
Pockets: 1 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	ADP compounds hydrolase nude (EC 3.6.1.-)	protein	185	20% helix, 44% strand	P45799

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1037	0.82	0.83	100	empty

Interfaces

1 interface between chains.

A–B · 2895 Å² buried · 44 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

1VHG · Crystal structure of ADP compounds hydrolase · the same entry in another collection · chain A against A, TM-score 1.00
P45799 · AlphaFold monomer V2.0 prediction for ADP compounds hydrolase nude (P45799) · a predicted model of the same protein · chain A 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 P45799
Elsewhere: RCSB PDB 1VHG · PDBe 1VHG · UniProt P45799

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