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The value crystal structure of apo quinone reductase 2 at 1.35A

Analyse The value crystal structure of apo quinone reductase 2 at 1.35A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4QOD
Type: protein
Length: 458 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribosyldihydronicotinamide dehydrogenase [quinone]
EC: 1.10.99.2
UniProt: P16083
Ligands: ZN
Pockets: 2 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ribosyldihydronicotinamide dehydrogenase [quinone] (EC 1.10.99.2)	protein	229	43% helix, 16% strand	P16083

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B
GOL · Glycerol · additive · 6 copies · chains A, B

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

Pockets

2 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	517	0.80	0.86	46	GOL
2	569	0.77	0.83	49	GOL

Interfaces

1 interface between chains.

A–B · 2080 Å² buried · 29 hydrogen bonds · protein-protein

Compared structures

4QOD · The value crystal structure of apo qui reductase 2 at 1.35A · 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 P16083
Elsewhere: RCSB PDB 4QOD · PDBe 4QOD · UniProt P16083

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