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Crystal structure of a. niger ochratoxinase

Analyse Crystal structure of a. niger ochratoxinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4C5Y
Type: protein
Length: 869 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ochratoxinase
EC: 3.4.13.9, 3.5.1.-
UniProt: A2R2V4
Ligands: ZN
Pockets: 12 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ochratoxinase (EC 3.4.13.9, 3.5.1.-)	protein	436	36% helix, 21% strand	A2R2V4
B	Ochratoxinase (EC 3.4.13.9, 3.5.1.-)	protein	433	36% helix, 21% strand	A2R2V4

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

12 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	784	0.79	0.82	69	ZN
2	678	0.77	0.82	57	ZN
3	264	0.58	0.78	39	empty
4	253	0.56	0.77	36	empty
5	128	0.45	0.77	28	empty

Interfaces

1 interface between chains.

A–B · 1935 Å² buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (carboxylation).

Compared structures

4C5Y · Crystal structure of A. niger ochratoxinase · 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 A2R2V4
Elsewhere: RCSB PDB 4C5Y · PDBe 4C5Y · UniProt A2R2V4

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