Research workbench

Crystal structure of tyrosinase from bacillus megaterium V218F mutant soaked in CUSO4

Analyse Crystal structure of tyrosinase from bacillus megaterium V218F mutant soaked in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HD6
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 0.75

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 6% strand (DSSP).

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

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

2 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	389	0.75	0.85	64	empty
2	51	0.33	0.78	16	empty

Interfaces

1 interface between chains.

A–B · 1137 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

4HD6 · Crystal Structure of Tyrosinase from Bacillus megaterium V218F mutant soaked in CuSO4 · 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 4HD6 · PDBe 4HD6 · UniProt B2ZB02

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.