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Crystal structure of tyrosinase from bacillus megaterium

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

PDB: 3NM8
Type: protein
Length: 570 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: ZN, CU, CL
Pockets: 4 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Tyrosinase (EC 1.14.18.1)	protein	285	42% helix, 5% strand	B2ZB02

Ligands and binding sites

ZN · Zinc ion · metal · 7 copies · chains A, B
CU · Copper (II) ion · metal · 4 copies · chains A, B
CL · Chloride ion · ion · 6 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	446	0.76	0.85	75	CU
2	101	0.44	0.79	22	CU
3	65	0.41	0.80	22	empty
4	53	0.27	0.74	17	CL

Interfaces

1 interface between chains.

A–B · 1066 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

3NM8 · Crystal structure of Tyrosinase from Bacillus megaterium · 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 3NM8 · PDBe 3NM8 · UniProt B2ZB02

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