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Crystal structure analysis of the ADP-ribose pyrophosphatase complexed with zn

Analyse Crystal structure analysis of the ADP-ribose pyrophosphatase complexed with zn in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1V8N
Type: protein
Length: 150 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ADP-ribose pyrophosphatase
EC: 3.6.1.13
UniProt: Q84CU3
Ligands: ZN
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ADP-ribose pyrophosphatase (EC 3.6.1.13)	protein	150	23% helix, 46% strand	Q84CU3

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	203	0.48	0.75	29	empty

Compared structures

1V8N · Crystal structure analysis of the ADP-ribose pyrophosphatase complexed with Zn · 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 Q84CU3
Elsewhere: RCSB PDB 1V8N · PDBe 1V8N · UniProt Q84CU3

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