Your browser does not support inline frames or is currently configured not to display inline frames. Content can be viewed at actual source page: inc/head.html
PDBsum entry 3npy
Go to PDB code:
Oxidoreductase
PDB id
3npy
Loading ...
Contents
Protein chains
281 a.a.
*
Metals
_CL
×6
_CU
×4
_ZN
×8
Waters
×172
*
Residue conservation analysis
PDB id:
3npy
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
ProSAT
Name:
Oxidoreductase
Title:
Crystal structure of tyrosinase from bacillus megaterium soaked in cuso4
Structure:
Tyrosinase. Chain: a, b. Engineered: yes
Source:
Bacillus megaterium. Organism_taxid: 1404. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.19Å
R-factor:
0.250
R-free:
0.275
Authors:
M.Sendovski,M.Kanteev,N.Adir,A.Fishman
Key ref:
M.Sendovski et al. (2011). First structures of an active bacterial tyrosinase reveal copper plasticity.
J Mol Biol
,
405
, 227-237.
PubMed id:
21040728
Date:
29-Jun-10
Release date:
17-Nov-10
PROCHECK
Headers
References
Protein chains
B2ZB02
(B2ZB02_PRIMG) - Tyrosinase from Priestia megaterium
Seq:
Struc:
297 a.a.
281 a.a.
Key:
Secondary structure
CATH domain
Enzyme reactions
Enzyme class:
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
reference
J Mol Biol
405
:227-237 (2011)
PubMed id:
21040728
First structures of an active bacterial tyrosinase reveal copper plasticity.
M.Sendovski,
M.Kanteev,
V.S.Ben-Yosef,
N.Adir,
A.Fishman.
ABSTRACT
No abstract given.
'); } }