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Crystal structure of a new type of NADPH-dependent quinone oxidoreductase (QOR2) from escherichia COLI

Analyse Crystal structure of a new type of NADPH-dependent quinone oxidoreductase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZCU
Type: protein
Length: 275 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized oxidoreductase ytfg
EC: 1.6.5.5
UniProt: P39315
Ligands: CU
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized oxidoreductase ytfg (EC 1.6.5.5)	protein	275	46% helix, 17% strand	P39315

Ligands and binding sites

CU · Copper (II) ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	193	0.51	0.77	27	empty
2	81	0.44	0.80	18	empty

Compared structures

2ZCU · Crystal structure of a new type of NADPH-dependent qui oxidoreductase (QOR2) from… · the same entry in another collection · chain A against A, TM-score 1.00
P39315 · AlphaFold monomer V2.0 prediction for quinone oxidoreductase 2 (P39315) · 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 P39315
Elsewhere: RCSB PDB 2ZCU · PDBe 2ZCU · UniProt P39315

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