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PDBsum entry 3a4z
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Oxidoreductase
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PDB id
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3a4z
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Oxidoreductase
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Title:
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Structure of cytochrome p450 vdh mutant (vdh-k1) obtained by directed evolution
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Structure:
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Vitamin d hydroxylase. Chain: a, b, c, d, e. Engineered: yes. Mutation: yes
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Source:
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Pseudonocardia autotrophica. Organism_taxid: 2074. Strain: nbrc 12743. Gene: vdh. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.20Å
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R-factor:
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0.203
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R-free:
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0.244
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Authors:
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Y.Yasutake,Y.Fujii,W.K.Cheon,A.Arisawa,T.Tamura
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Key ref:
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Y.Yasutake
et al.
(2010).
Structural evidence for enhancement of sequential vitamin D3 hydroxylation activities by directed evolution of cytochrome P450 vitamin D3 hydroxylase.
J Biol Chem,
285,
31193-31201.
PubMed id:
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Date:
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24-Jul-09
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Release date:
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28-Jul-10
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PROCHECK
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Headers
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References
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C4B644
(CPVDH_PSEAH) -
Vitamin D(3) 25-hydroxylase from Pseudonocardia autotrophica
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Seq:
Struc:
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403 a.a.
402 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 4 residue positions (black
crosses)
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Enzyme class:
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E.C.1.14.15.15
- cholestanetriol 26-monooxygenase.
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Reaction:
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5beta-cholestane-3alpha,7alpha,12alpha-triol + 6 reduced [adrenodoxin] + 3 O2 + 5 H+ = (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan- 26-oate + 6 oxidized [adrenodoxin] + 4 H2O
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5beta-cholestane-3alpha,7alpha,12alpha-triol
Bound ligand (Het Group name = )
matches with 62.22% similarity
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6
×
reduced [adrenodoxin]
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+
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3
×
O2
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+
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5
×
H(+)
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=
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(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan- 26-oate
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+
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6
×
oxidized [adrenodoxin]
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+
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4
×
H2O
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Cofactor:
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Heme-thiolate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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J Biol Chem
285:31193-31201
(2010)
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PubMed id:
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Structural evidence for enhancement of sequential vitamin D3 hydroxylation activities by directed evolution of cytochrome P450 vitamin D3 hydroxylase.
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Y.Yasutake,
Y.Fujii,
T.Nishioka,
W.K.Cheon,
A.Arisawa,
T.Tamura.
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ABSTRACT
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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R.Brandman,
J.N.Lampe,
Y.Brandman,
and
P.R.de Montellano
(2011).
Active-site residues move independently from the rest of the protein in a 200 ns molecular dynamics simulation of cytochrome P450 CYP119.
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Arch Biochem Biophys,
509,
127-132.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
