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Crystal structure of aldo-keto reductase from sinorhizobium meliloti 1021 in complex with NADPH

Analyse Crystal structure of aldo-keto reductase from sinorhizobium meliloti 1021 in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5C7H
Type: protein
Length: 281 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aldo-keto reductase
EC: 1.1.1.-
UniProt: Q92NR7
Ligands: NDP
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aldo-keto reductase (EC 1.1.1.-)	protein	281	47% helix, 15% strand	Q92NR7

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	205	0.62	0.82	31	NDP

Compared structures

5C7H · Crystal structure of aldo-keto reductase from Sinorhizobium meliloti 1021 in complex with… · 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 Q92NR7
Elsewhere: RCSB PDB 5C7H · PDBe 5C7H · UniProt Q92NR7

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