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Crystal structure of aldo-keto reductase from agrobacterium tumefaciens in a ternary complex with NADPH and glucose

Analyse Crystal structure of aldo-keto reductase from agrobacterium tumefaciens in a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BC1
Type: protein
Length: 295 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aryl-alcohol dehydrogenase
UniProt: A9CEY6
Ligands: NAP, GLC
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aryl-alcohol dehydrogenase	protein	295	44% helix, 18% strand	A9CEY6

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
GLC · alpha-D-glucopyranose · sugar · 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	226	0.62	0.82	37	NAP, GLC
2	51	0.31	0.76	10	empty

Compared structures

7BC1 · Crystal structure of aldo-keto reductase from Agrobacterium tumefaciens in a ternary… · 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 A9CEY6
Elsewhere: RCSB PDB 7BC1 · PDBe 7BC1 · UniProt A9CEY6

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