MolNFT v1 · #108738 · protein

Crystal structure of ALDO/KETO reductase from klebsiella pneumoniae in complex with NADP and acetate at 1.8 a resolution

4WGH · Aldehyde reductase: “Crystal structure of ALDO/KETO reductase from klebsiella pneumoniae in complex with NADP and acetate at 1.8 a…”. X-ray diffraction, 1 ligand (NAP), 2 pockets (best druggability 0.65). MolNFT v1 #108738 on…

PDB: 4WGH
Type: protein
Length: 283 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aldehyde reductase
UniProt: V3S9R5
Ligands: NAP
Pockets: 2 · best druggability 0.65

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aldehyde reductase	protein	283	43% helix, 16% strand	V3S9R5

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
ACT · Acetate ion · additive · 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	221	0.65	0.83	35	NAP, ACT
2	50	0.25	0.73	18	empty

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

4WGH · Crystal structure of aldo/keto reductase from Klebsiella pneumoniae in complex with NADP… · 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 V3S9R5
Elsewhere: RCSB PDB 4WGH · PDBe 4WGH · UniProt V3S9R5

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