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Human Aldose Reductase complexed with four tolrestat molecules at 1.5 A resolution.

Analyse Human Aldose Reductase complexed with four tolrestat molecules at 1.5 A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FZB
Type: protein
Length: 316 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.5
Source: Homo sapiens
Molecule: aldose reductase
EC: 1.1.1.21
UniProt: Q5U031
Ligands: TOL, NAP
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · resolution 1.5 · 1 distinct chain · 39% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	aldose reductase (EC 1.1.1.21)	protein	316	39% helix, 15% strand	Q5U031

Ligands and binding sites

TOL · Tolrestat · ligand · 4 copies · chains A
NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 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	329	0.74	0.85	49	NAP, TOL
2	62	0.46	0.84	19	empty

Compared structures

2FZB · Human aldose reductase complexed with four tolrestat molecules at 1.5 a resolution. · 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 2FZB · PDBe 2FZB · UniProt Q5U031

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