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Crystal structure of the tyrosinase pvdp from pseudomonas aeruginosa

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

PDB: 6RRR
Type: protein
Length: 932 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pvdp
UniProt: Q9I188
Pockets: 13 · best druggability 0.87

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pvdp	protein	472	37% helix, 15% strand	Q9I188
B	Pvdp	protein	460	40% helix, 15% strand	Q9I188

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

13 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	1068	0.87	0.89	104	GOL
2	66	0.50	0.85	22	empty
3	81	0.46	0.81	20	empty
4	145	0.45	0.76	25	empty
5	150	0.45	0.76	22	empty

Interfaces

1 interface between chains.

A–B · 3453 Å² buried · 41 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (artifact).

Compared structures

6RRR · Crystal structure of the tyrosinase PvdP from Pseudomonas aeruginosa · 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 Q9I188
Elsewhere: RCSB PDB 6RRR · PDBe 6RRR · UniProt Q9I188

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