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Citrate bound, C298A/W219Y mutant human aldose reductase

Analyse Citrate bound, C298A/W219Y mutant human aldose reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1AZ2
Type: protein
Length: 314 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aldose reductase
EC: 1.1.1.21
UniProt: P15121
Ligands: NAP
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aldose reductase (EC 1.1.1.21)	protein	314	31% helix, 16% strand	P15121

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
CIT · Citric acid · 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	307	0.70	0.83	43	NAP, CIT
2	94	0.45	0.80	19	empty

Compared structures

1AZ2 · Citrate bound, C298A/W219Y mutant human aldose reductase · the same entry in another collection · chain A against A, TM-score 1.00
P15121 · AlphaFold monomer V2.0 prediction for aldo-keto reductase family 1 member B1 (P15121) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P15121
Elsewhere: RCSB PDB 1AZ2 · PDBe 1AZ2 · UniProt P15121

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