MolNFT v1 · #153898 · protein

Aspergillus oryzae pro-tyrosinase F513Y mutant

6JU4: “Aspergillus oryzae pro-tyrosinase F513Y mutant”. X-ray diffraction, 1 ligand (CU), 15 pockets (best druggability 0.76). MolNFT v1 #153898 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6JU4
Type: protein
Length: 1,101 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosinase
EC: 1.14.18.1
UniProt: A0A1S9DK56
Ligands: CU
Pockets: 15 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosinase (EC 1.14.18.1)	protein	541	36% helix, 16% strand	A0A1S9DK56
B	Tyrosinase (EC 1.14.18.1)	protein	560	36% helix, 17% strand	A0A1S9DK56

Ligands and binding sites

CU · Copper (II) ion · metal · 4 copies · chains A, 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	100	0.76	0.97	28	empty
2	95	0.76	0.96	19	empty
3	56	0.70	0.98	23	empty
4	57	0.70	0.97	19	empty
5	610	0.65	0.76	38	empty

Interfaces

1 interface between chains.

A–B · 1770 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

6JU4 · Aspergillus oryzae pro-tyrosinase F513Y 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 6JU4 · PDBe 6JU4 · UniProt A0A1S9DK56

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