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Crystal structure of an oxidoreductase from burkholderia vietnamiensis in complex with NADP

Analyse Crystal structure of an oxidoreductase from burkholderia vietnamiensis in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5IDW
Type: protein
Length: 450 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Short-chain DEHYDROGENASE/REDUCTASE sdr
UniProt: A4JIB1
Ligands: NAP
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Short-chain DEHYDROGENASE/REDUCTASE sdr	protein	225	46% helix, 16% strand	A4JIB1

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 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	365	0.72	0.84	40	NAP
2	333	0.70	0.83	40	NAP

Interfaces

1 interface between chains.

A–B · 1811 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

5IDW · Crystal structure of an oxidoreductase from Burkholderia vietnamiensis in complex with… · 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 A4JIB1
Elsewhere: RCSB PDB 5IDW · PDBe 5IDW · UniProt A4JIB1

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