Structure of PDB 2vn0 Chain A

Receptor sequence
>2vn0A (length=464) Species: 9606 (Homo sapiens) [Search protein sequence]
KLPPGPTPLPIIGNMLQIDVKDICKSFTNFSKVYGPVFTVYFGMNPIVVF
HGYEAVKEALIDNGEEFSGRGNSPISQRITKGLGIISSNGKRWKEIRRFS
LTTLRNFGMGKRSIEDRVQEEAHCLVEELRKTKASPCDPTFILGCAPCNV
ICSVVFQKRFDYKDQNFLTLMKRFNENFRILNSPWIQVCNNFPLLIDCFP
GTHNKVLKNVALTRSYIREKVKEHQASLDVNNPRDFIDCFLIKMEQEKDN
QKSEFNIENLVGTVADLFVAGTETTSTTLRYGLLLLLKHPEVTAKVQEEI
DHVIGRHRSPCMQDRSHMPYTDAVVHEIQRYSDLVPTGVPHAVTTDTKFR
NYLIPKGTTIMALLTSVLHDDKEFPNPNIFDPGHFLDKNGNFKKSDYFMP
FSAGKRICAGEGLARMELFLFLTTILQNFNLKSVDDLKNLNTTAVTKGIV
SLPPSYQICFIPVH
3D structure
PDB2vn0 Determinants of cytochrome P450 2C8 substrate binding: structures of complexes with montelukast, troglitazone, felodipine, and 9-cis-retinoic acid.
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T301 F428 C435
Catalytic site (residue number reindexed from 1) T274 F401 C408
Enzyme Commision number 1.14.14.1: unspecific monooxygenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEM A R97 I112 W120 R124 A297 G298 T301 T302 H368 P427 F428 S429 R433 C435 A436 G437 R70 I85 W93 R97 A270 G271 T274 T275 H341 P400 F401 S402 R406 C408 A409 G410
BS02 TDZ A I106 N204 F205 L208 N209 R241 V296 E300 I79 N177 F178 L181 N182 R214 V269 E273
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0008392 arachidonate epoxygenase activity
GO:0008401 retinoic acid 4-hydroxylase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0016712 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
GO:0020037 heme binding
GO:0034875 caffeine oxidase activity
GO:0046872 metal ion binding
GO:0070330 aromatase activity
GO:0101020 estrogen 16-alpha-hydroxylase activity
Biological Process
GO:0002933 lipid hydroxylation
GO:0006082 organic acid metabolic process
GO:0006805 xenobiotic metabolic process
GO:0008202 steroid metabolic process
GO:0008210 estrogen metabolic process
GO:0019369 arachidonate metabolic process
GO:0019373 epoxygenase P450 pathway
GO:0042178 xenobiotic catabolic process
GO:0042572 retinol metabolic process
GO:0042573 retinoic acid metabolic process
GO:0042759 long-chain fatty acid biosynthetic process
GO:0046456 icosanoid biosynthetic process
GO:0070989 oxidative demethylation
GO:0097267 omega-hydroxylase P450 pathway
Cellular Component
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0043231 intracellular membrane-bounded organelle

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2vn0, PDBe:2vn0, PDBj:2vn0
PDBsum2vn0
PubMed18413310
UniProtP10632|CP2C8_HUMAN Cytochrome P450 2C8 (Gene Name=CYP2C8)

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