MolNFT v1 · #141594 · protein

Crystal structure of xylose reductase from debaryomyces nepalensis in complex with NADP-dtt adduct

5ZCM · Aldose reductase: “Crystal structure of xylose reductase from debaryomyces nepalensis in complex with NADP-dtt adduct”. X-ray diffraction, 1 ligand (NDP), 2 pockets (best druggability 0.71). MolNFT v1 #141594 on GenesisL1: 3D…

PDB: 5ZCM
Type: protein
Length: 329 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aldose reductase
EC: 1.1.1.21
UniProt: A0A0M4HL56
Ligands: NDP
Pockets: 2 · best druggability 0.71

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aldose reductase (EC 1.1.1.21)	protein	329	39% helix, 15% strand	A0A0M4HL56

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
DTT · 2,3-dihydroxy-1,4-dithiobutane · 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	321	0.71	0.84	47	NDP, DTT
2	50	0.27	0.74	16	empty

Compared structures

5ZCM · Crystal structure of Xylose reductase from Debaryomyces nepalensis 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 A0A0M4HL56
Elsewhere: RCSB PDB 5ZCM · PDBe 5ZCM · UniProt A0A0M4HL56

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.