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Crystal structure of tyrosinase caddy PROTEIN(MELC1)WITH tyrosinase (MELC2)FROM streptomyces avermitilis in complex with zinc ion

Analyse Crystal structure of tyrosinase caddy PROTEIN(MELC1)WITH tyrosinase (MELC2)FROM… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6J2U
Type
protein
Length
345 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tyrosinase co-factor protein; Tyrosinase
UniProt
Q93HL1, Q93HL2
Ligands
ZN
Pockets
1 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATyrosinase co-factor proteinprotein7217% helix, 46% strandQ93HL1
BTyrosinaseprotein27342% helix, 4% strandQ93HL2

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11060.460.8022empty

Interfaces

1 interface between chains.

  • A–B · 1018 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 6J2U · Crystal structure of Tyrosinase caddy protein(MelC1)with Tyrosinase (MelC2)from… · the same entry in another collection · chain A against A, TM-score 1.00

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