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Crystal structure of tyrosinase from bacillus megaterium N205D mutant

Analyse Crystal structure of tyrosinase from bacillus megaterium N205D mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4J6V
Type: protein
Length: 573 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosinase
EC: 1.14.18.1
UniProt: B2ZB02
Ligands: CU
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosinase (EC 1.14.18.1)	protein	286	42% helix, 6% strand	B2ZB02
B	Tyrosinase (EC 1.14.18.1)	protein	287	44% helix, 5% strand	B2ZB02

Ligands and binding sites

CU · Copper (II) ion · metal · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	210	0.63	0.83	46	empty
2	190	0.61	0.82	43	empty

Interfaces

1 interface between chains.

A–B · 1134 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

4J6V · Crystal Structure of Tyrosinase from Bacillus megaterium N205D 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 B2ZB02
Elsewhere: RCSB PDB 4J6V · PDBe 4J6V · UniProt B2ZB02

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