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Crystal structure of apo form of xylose reductase from debaryomyces nepalensis

Analyse Crystal structure of apo form of xylose reductase from debaryomyces nepalensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZCI
Type: protein
Length: 642 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aldose reductase
EC: 1.1.1.21
UniProt: A0A0M4HL56
Pockets: 9 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aldose reductase (EC 1.1.1.21)	protein	320	40% helix, 15% strand	A0A0M4HL56
B	Aldose reductase (EC 1.1.1.21)	protein	322	39% helix, 15% strand	A0A0M4HL56

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	620	0.73	0.80	48	empty
2	58	0.56	0.89	19	empty
3	179	0.56	0.80	28	empty
4	139	0.51	0.79	21	empty
5	75	0.43	0.80	15	empty

Interfaces

1 interface between chains.

A–B · 1377 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

5ZCI · Crystal structure of apo form of Xylose reductase from Debaryomyces nepalensis · 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 5ZCI · PDBe 5ZCI · UniProt A0A0M4HL56

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