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Crystal structure of an oxidoreductase, short-chain DEHYDROGENASE/REDUCTASE family protein from brucella suis

Analyse Crystal structure of an oxidoreductase, short-chain DEHYDROGENASE/REDUCTASE… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4NPC
Type: protein
Length: 504 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sorbitol dehydrogenase
UniProt: B0CIA7
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sorbitol dehydrogenase	protein	251	49% helix, 16% strand	B0CIA7
B	Sorbitol dehydrogenase	protein	253	49% helix, 16% strand	B0CIA7

Ligands and binding sites

ACT · Acetate ion · additive · 2 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	477	0.71	0.81	50	ACT
2	494	0.70	0.80	45	ACT

Interfaces

1 interface between chains.

A–B · 1517 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

4NPC · Crystal Structure of an Oxidoreductase, Short-Chain Dehydrogenase/Reductase Family… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt B0CIA7
Elsewhere: RCSB PDB 4NPC · PDBe 4NPC · UniProt B0CIA7

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