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Determination of the structure of active tyrosinase from bacterium Verrucomicrobium spinosum

Analyse Determination of the structure of active tyrosinase from bacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8BBQ
Type: protein
Length: 645 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.43
Source: Verrucomicrobium spinosum
Molecule: Core tyrosinase
EC: 1.14.18.1
Ligands: CU, SO4
Pockets: 6 · best druggability 0.68

Structure

x-ray diffraction · resolution 1.43 · 2 distinct chains · 53% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Core tyrosinase (EC 1.14.18.1)	protein	324	52% helix, 5% strand	—
B	Core tyrosinase (EC 1.14.18.1)	protein	321	53% helix, 5% strand	—

Ligands and binding sites

CU · Copper (II) ion · metal · 4 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains A, B
GOL · Glycerol · additive · 7 copies · chains A, B

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

Pockets

6 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	429	0.68	0.80	49	empty
2	420	0.64	0.78	48	empty
3	70	0.45	0.82	19	GOL
4	58	0.41	0.81	18	GOL
5	111	0.38	0.74	23	SO4, GOL

Interfaces

1 interface between chains.

A–B · 701 Å² buried · 12 hydrogen bonds · protein-protein

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 8BBQ · PDBe 8BBQ

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