› 5m8r

X-ray diffraction
2.4Å resolution

Crystal structure of human tyrosinase related protein 1 (T391V-R374S-Y362F) in complex with mimosine

Released:
DOI: 10.2210/pdb5m8r/pdb
PDB entry 5m8r coloured by chain, front view.
PDB entry 5m8r coloured by chain, side view.
PDB entry 5m8r 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
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 (5 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: 50.53 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
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
3 bound ligands:
Ligand NAG 11 x NAG
Ligand ZN 9 x ZN
Ligand MMS 4 x MMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-1
Spacegroup: P212121
Unit cell:
a: 89.353Å b: 139.727Å c: 190.951Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.2 0.249
Expression system: Spodoptera frugiperda

Quick links

Citations

8 review citations

Recent advances in screening active components from natural products based on bioaffinity techniques.
Hou et al. (2020)
7 more

3 mentions without citation

Phenylthiourea Binding to Human Tyrosinase-Related Protein 1.
Lai et al. (2020)
2 more