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Aspergillus oryzae pro-tyrosinase oxygen-bound C92A mutant

Analyse Aspergillus oryzae pro-tyrosinase oxygen-bound C92A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6JUA
Type: protein
Length: 1,089 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.45
Source: Aspergillus oryzae
Molecule: Tyrosinase
EC: 1.14.18.1
UniProt: A0A1S9DK56
Ligands: CU, PER
Pockets: 15 · best druggability 0.78

Structure

x-ray diffraction · resolution 1.45 · 2 distinct chains · 36% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosinase (EC 1.14.18.1)	protein	533	37% helix, 16% strand	A0A1S9DK56
B	Tyrosinase (EC 1.14.18.1)	protein	556	36% helix, 16% strand	A0A1S9DK56

Ligands and binding sites

CU · Copper (II) ion · metal · 4 copies · chains A, B
PER · Peroxide ion · ion · chains B

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

Pockets

15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	118	0.78	0.97	28	empty
2	1034	0.75	0.78	93	empty
3	58	0.72	0.99	19	empty
4	59	0.70	0.97	20	empty
5	438	0.68	0.80	54	empty

Interfaces

1 interface between chains.

A–B · 1597 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

6JUA · Aspergillus oryzae pro-tyrosinase oxygen-bound C92A mutant · 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 A0A1S9DK56
Elsewhere: RCSB PDB 6JUA · PDBe 6JUA · UniProt A0A1S9DK56

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