Research workbench

Human aldose reductase in complex with NADP and citrate at 0.82 ångström

Analyse Human aldose reductase in complex with NADP and citrate at 0.82 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2J8T
Type: protein
Length: 316 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aldo-keto reductase family 1, member B1
EC: 1.1.1.21
UniProt: Q5U031
Ligands: NAP
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aldo-keto reductase family 1, member B1 (EC 1.1.1.21)	protein	316	39% helix, 15% strand	Q5U031

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
FLC · Citrate anion · additive · 2 copies · 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	335	0.69	0.82	48	NAP, FLC

Compared structures

2J8T · Human aldose reductase in complex with NADP and citrate at 0.82 angstrom · 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 Q5U031
Elsewhere: RCSB PDB 2J8T · PDBe 2J8T · UniProt Q5U031

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