› 5m8o

X-ray diffraction
2.5Å resolution

Crystal structure of human tyrosinase related protein 1 in complex with tropolone

Released:
DOI: 10.2210/pdb5m8o/pdb
PDB entry 5m8o coloured by chain, front view.
PDB entry 5m8o coloured by chain, side view.
PDB entry 5m8o coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of Human Tyrosinase Related Protein 1 Reveals a Binuclear Zinc Active Site Important for Melanogenesis.
Lai X, Wichers HJ, Soler-Lopez M, Dijkstra BW
OpenAccess logo Angew Chem Int Ed Engl 56 9812-9815 (2017)
PMID: 28661582

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148124 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (8 distinct):
5,6-dihydroxyindole-2-carboxylic acid oxidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 446 amino acids
Theoretical weight: 50.62 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P17643 (Residues: 25-470; Coverage: 87%)
Gene names: CAS2, TYRP, TYRP1, TYRRP
Sequence domains: Common central domain of tyrosinase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer
2 bound ligands:
Ligand 0TR 4 x 0TR
Ligand ZN 8 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 89.688Å b: 140.202Å c: 191.058Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.204 0.251
Expression system: Spodoptera frugiperda

Quick links

Citations

9 review citations

Structure and Function of Human Tyrosinase and Tyrosinase-Related Proteins.
Lai et al. (2018)
8 more

3 mentions without citation

Novel Quercetin Derivative of 3,7-Dioleylquercetin Shows Less Toxicity and Highly Potent Tyrosinase Inhibition Activity.
Choi et al. (2021)
2 more