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PDBsum entry 2zwf

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase/metal transport PDB id
2zwf

 

 

 

 

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Contents
Protein chains
276 a.a. *
72 a.a. *
Ligands
NO3 ×5
Metals
_CU ×4
Waters ×424
* Residue conservation analysis
PDB id:
2zwf
Name: Oxidoreductase/metal transport
Title: Crystal structure of the copper-bound tyrosinase in complex with a caddie protein from streptomyces castaneoglobisporus obtained by soaking the deoxy-form crystal in dioxygen-saturated solution for 80 minutes
Structure: Tyrosinase. Chain: a. Engineered: yes. Melc. Chain: b. Synonym: caddie protein orf378. Engineered: yes
Source: Streptomyces castaneoglobisporus. Organism_taxid: 79261. Strain: hut 6202. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
1.40Å     R-factor:   0.173     R-free:   0.212
Authors: Y.Matoba,M.Sugiyama
Key ref: Y.Matoba et al. Crystallographic evidence of drastic movement of a copper ion toward the substrate tyrosine for starting hydroxylation reaction of tyrosinase. To be published, .
Date:
03-Dec-08     Release date:   15-Dec-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Q83WS2  (Q83WS2_9ACTN) -  Tyrosinase from Streptomyces castaneoglobisporus
Seq:
Struc:
273 a.a.
276 a.a.*
Protein chain
Q83WS1  (Q83WS1_9ACTN) -  MelC from Streptomyces castaneoglobisporus
Seq:
Struc:
126 a.a.
72 a.a.*
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain A: E.C.1.14.18.1  - tyrosinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Melanin Biosynthesis
      Reaction:
1. L-tyrosine + O2 = L-dopaquinone + H2O
2. 2 L-dopa + O2 = 2 L-dopaquinone + 2 H2O
L-tyrosine
+ O2
= L-dopaquinone
+ H2O
2 × L-dopa
+ O2
= 2 × L-dopaquinone
+ 2 × H2O
      Cofactor: Cu cation
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

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