Structure of PDB 1n6b Chain A

Receptor sequence
>1n6bA (length=462) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
GKLPPGPTPFPIIGNILQIDAKDISKSLTKFSECYGPVFTVYLGMKPTVV
LHGYEAVKEALVDLGEEFAGRGSVPILEKVSKGLGIAFSNAKTWKEMRRF
SLMTLRNFGMGKRSIEDRIQEEARCLVEELRKTNASPCDPTFILGCAPCN
VICSVIFHNRFDYKDEEFLKLMESLHENVELLGTPWLQVYNNFPALLDYF
PGIHKTLLKNADYIKNFIMEKVKEHQKLLDVNNPRDFIDCFLIKMEQENN
LEFTLESLVIAVSDLFGAGTETTSTTLRYSLLLLLKHPEVAARVQEEIER
VIGRHRSPCMQDRSRMPYTDAVIHEIQRFIDLLPTNLPHAVTRDVRFRNY
FIPKGTDIITSLTSVLHDEKAFPNPKVFDPGHFLDESGNFKKSDYFMPFS
AGKRMCVGEGLARMELFLFLTSILQNFKLQSLVEPKDLDITAVVNGFVSV
PPSYQLCFIPIH
3D structure
PDB1n6b Structure of a Substrate Complex of Mammalian Cytochrome P450 2C5 at 2.3 A Resolution: Evidence for Multiple Substrate Binding Modes
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) T298 F425 C432
Catalytic site (residue number reindexed from 1) T272 F399 C406
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 R124 A294 G295 T298 N362 H365 P424 F425 S426 R430 C432 G434 R71 R98 A268 G269 T272 N336 H339 P398 F399 S400 R404 C406 G408
BS02 DMZ A F114 N204 V205 G293 A294 L363 F473 F88 N178 V179 G267 A268 L337 F447 MOAD: Kd=20uM
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
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:0046872 metal ion binding
GO:0070330 aromatase activity
Biological Process
GO:0006082 organic acid metabolic process
GO:0006805 xenobiotic metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0016020 membrane
GO:0043231 intracellular membrane-bounded organelle

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1n6b, PDBe:1n6b, PDBj:1n6b
PDBsum1n6b
PubMed12767218
UniProtP00179|CP2C5_RABIT Cytochrome P450 2C5 (Gene Name=CYP2C5)

[Back to BioLiP]