Uniprot accession / id : P56656  OR   Uniprot accession / id : P10632
 
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Entry Information
Entry status  (1)
REL
(5)
 
Experimental methods  (1)
X-ray diffraction
(5)
 
Authors  (8)
Johnson EF
(5)
Schoch GA
(5)
Stout CD
(5)
Yano JK
(5)
Dansette PM
(4)
Sansen S
(4)
Griffin KJ
(1)
Wester MR
(1)
 
Homo / hetero assembly  (1)
homo
(5)
 
Assembly composition  (1)
protein structure
(5)
 
Assembly polymer count  (1)
monomer
(5)
 
Resolution distribution
2.0 - 2.5
(1)
2.5 - 3
(4)
 
Release year distribution
2000 - 2005
(1)
2005 - 2010
(4)
 
Journal  (1)
J Biol Chem
(5)
 
Macromolecules
Organism superkingdom  (1)
Eukaryota
(5)
 
Organism name  (1)
Homo sapiens
(5)
 
Molecule name  (7)
CYPIIC8
(5)
Cytochrome P450 2C8
(5)
Cytochrome P450 IIC2
(5)
Cytochrome P450 MP-12
(5)
Cytochrome P450 MP-20
(5)
Cytochrome P450 form 1
(5)
S-mephenytoin 4-hydroxylase
(5)
 
Molecule type  (1)
Protein
(5)
 
Gene names  (1)
CYP2C8
(5)
 
Interacting ligands  (8)
HEM : PROTOPORPHYRIN IX CONTAINING FE
(5)
PLM : PALMITIC ACID
(5)
SO4 : SULFATE ION
(3)
225 : FELODIPINE
(1)
9CR : (9cis)-retinoic acid
(1)
MTK : MONTELUKAST
(1)
PO4 : PHOSPHATE ION
(1)
TDZ : (5R)-5-(4-{[(2R)-6-HYDROXY-2,5,7,8-TETRAMETHYL-3,4-DIHYDRO-2H-CHROMEN-2-YL]METHOXY}BENZYL)-1,3-THIAZOLIDINE-2,4-DIONE
(1)
 
Function and Biology
EC number / name  (1)
1.14.14.1 : Unspecific monooxygenase
(5)
 
Biological function  (12)
arachidonate epoxygenase activity
(5)
caffeine oxidase activity
(5)
estrogen 16-alpha-hydroxylase activity
(5)
heme binding
(5)
iron ion binding
(5)
metal ion binding
(5)
monooxygenase activity
(5)
oxidoreductase activity
(5)
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
(5)
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
(5)
protein binding
(5)
retinoic acid 4-hydroxylase activity
(5)
 
Biological process  (15)
arachidonate metabolic process
(5)
epoxygenase P450 pathway
(5)
estrogen metabolic process
(5)
icosanoid biosynthetic process
(5)
lipid hydroxylation
(5)
lipid metabolic process
(5)
long-chain fatty acid biosynthetic process
(5)
omega-hydroxylase P450 pathway
(5)
organic acid metabolic process
(5)
oxidative demethylation
(5)
retinoic acid metabolic process
(5)
retinol metabolic process
(5)
steroid metabolic process
(5)
xenobiotic catabolic process
(5)
xenobiotic metabolic process
(5)
 
Biological cell component  (6)
cytoplasm
(5)
endoplasmic reticulum
(5)
endoplasmic reticulum membrane
(5)
intracellular membrane-bounded organelle
(5)
membrane
(5)
plasma membrane
(5)
 
Compound cofactor class  (1)
Heme
(5)
 
Sequence and Structure classification
SCOP fold  (1)
Cytochrome P450
(5)
 
SCOP family  (1)
Cytochrome P450
(5)
 
CATH class  (1)
Mainly Alpha
(5)
 
CATH topology  (1)
Cytochrome p450
(5)
 
Pfam accession / name  (1)
PF00067 : p450
(5)
 
Experimental Information
Diffraction protocol  (1)
Single wavelength
(5)
 
Diffraction radiation source type  (2)
Synchrotron
(4)
Rotating anode
(1)
 
Diffraction source  (5)
RIGAKU
(1)
SSRL BEAMLINE BL1-5
(1)
SSRL BEAMLINE BL11-1
(1)
SSRL BEAMLINE BL7-1
(1)
SSRL BEAMLINE BL9-1
(1)
 
Synchrotron site  (1)
SSRL
(4)
 
Diffraction detector type  (2)
CCD
(3)
Image plate
(2)
 
Refinement software  (1)
CNS
(5)
 
Representative Structures
Representative Structures
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30%
Entries 1 to 5 of 5
Entries 1 to 5 of 5
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CYP2C8dH complexed with felodipine
Schoch GA, Yano JK, Stout CD, Johnson EF
J Biol Chem (2008) [PMID: 18413310  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: HEM    225    225    HEM    PLM    SO4   
Assembly name: Cytochrome P450 2C8 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-145365 (Preferred)   search this ID
PDBe-KB: P10632   
X-ray diffraction
2.28Å resolution
Released: 23 Oct 2007
Model geometry
Fit model/data
2nnj
2nnj
2nnj
Crystal Structure of Human Drug Metabolizing Cytochrome P450 2C8
Schoch GA, Yano JK, Wester MR, Griffin KJ, Stout CD, Johnson EF
J Biol Chem (2004) [PMID: 14676196  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: HEM    HEM    PLM    PO4   
Assembly name: Cytochrome P450 2C8 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-145365 (Preferred)   search this ID
PDBe-KB: P10632   
X-ray diffraction
2.7Å resolution
Released: 13 Jan 2004
Model geometry
Fit model/data
1pq2
1pq2
1pq2
CYP2C8DH COMPLEXED WITH TROGLITAZONE
Schoch GA, Yano JK, Sansen S, Stout CD, Johnson EF
J Biol Chem (2008) [PMID: 18413310  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: HEM    TDZ    HEM    PLM    TDZ   
Assembly name: Cytochrome P450 2C8 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-145365 (Preferred)   search this ID
PDBe-KB: P10632    P10632   
X-ray diffraction
2.7Å resolution
Released: 29 Apr 2008
Model geometry
Fit model/data
2vn0
2vn0
2vn0
CYP2C8dH complexed with montelukast
Schoch GA, Yano JK, Stout CD, Johnson EF
J Biol Chem (2008) [PMID: 18413310  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: HEM    HEM    PLM    SO4    MTK   
Assembly name: Cytochrome P450 2C8 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-145365 (Preferred)   search this ID
PDBe-KB: P10632   
X-ray diffraction
2.8Å resolution
Released: 23 Oct 2007
Model geometry
Fit model/data
2nni
2nni
2nni
CYP2C8dH complexed with 2 molecules of 9-cis retinoic acid
Schoch GA, Yano JK, Stout CD, Johnson EF
J Biol Chem (2008) [PMID: 18413310  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: HEM    9CR    9CR    HEM    PLM    SO4   
Assembly name: Cytochrome P450 2C8 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-145365 (Preferred)   search this ID
PDBe-KB: P10632   
X-ray diffraction
2.6Å resolution
Released: 23 Oct 2007
Model geometry
Fit model/data
2nnh
2nnh
2nnh
Entries 1 to 5 of 5
Entries 1 to 5 of 5