Structure of PDB 4nz2 Chain B

Receptor sequence
>4nz2B (length=464) Species: 9606 (Homo sapiens) [Search protein sequence]
KGRPPGPTPLPVIGNILQIGIKDISKSLTNLSKVYGPVFTLYFGLKPIVV
LHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKWKEIRRF
SLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCN
VICSIIFHKRFDYKDQQFLNLMEKLNENIEILSSPWIQVYNNFPALLDYF
PGTHNKLLKNVAFMKSYILEKVKEHQESMDMNNPQDFIDCFLMKMEKEKH
NQPSEFTIESLENTAVDLFGAGTETTSTTLRYALLLLLKHPEVTAKVQEE
IERVIGRNRSPCMQDRSHMPYTDAVVHEVQRYIDLLPTSLPHAVTCDIKF
RNYLIPKGTTILISLTSVLHDNKEFPNPEMFDPHHFLDEGGNFKKSKYFM
PFSAGKRICVGEALAGMELFLFLTSILQNFNLKSLVDPKNLDTTPVVNGF
ASVPPFYQLCFIPV
3D structure
PDB4nz2 Structure-based ligand design to overcome CYP inhibition in drug discovery projects.
ChainB
Resolution2.45 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) T275 F402 C409
Enzyme Commision number 1.14.14.1: unspecific monooxygenase.
1.14.14.51: (S)-limonene 6-monooxygenase.
1.14.14.52: (S)-limonene 7-monooxygenase.
1.14.14.53: (R)-limonene 6-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 B R97 I112 V113 R124 A297 G298 T301 L362 S365 L366 H368 P427 F428 S429 R433 C435 G437 A441 R71 I86 V87 R98 A271 G272 T275 L336 S339 L340 H342 P401 F402 S403 R407 C409 G411 A415
BS02 2QJ B N107 F114 I205 V237 G296 N81 F88 I179 V211 G270 MOAD: Kd=2uM
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0008392 arachidonate epoxygenase activity
GO:0008395 steroid hydroxylase activity
GO:0008404 arachidonate 14,15-epoxygenase activity
GO:0008405 arachidonate 11,12-epoxygenase activity
GO:0016491 oxidoreductase 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:0018675 (S)-limonene 6-monooxygenase activity
GO:0018676 (S)-limonene 7-monooxygenase activity
GO:0020037 heme binding
GO:0034875 caffeine oxidase activity
GO:0046872 metal ion binding
GO:0052741 (R)-limonene 6-monooxygenase activity
GO:0070330 aromatase activity
Biological Process
GO:0006805 xenobiotic metabolic process
GO:0008202 steroid metabolic process
GO:0008203 cholesterol metabolic process
GO:0008210 estrogen metabolic process
GO:0016098 monoterpenoid metabolic process
GO:0019369 arachidonate metabolic process
GO:0019373 epoxygenase P450 pathway
GO:0019627 urea metabolic process
GO:0032787 monocarboxylic acid metabolic process
GO:0042178 xenobiotic catabolic process
GO:0042759 long-chain fatty acid biosynthetic process
GO:0043603 amide metabolic 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:4nz2, PDBe:4nz2, PDBj:4nz2
PDBsum4nz2
PubMed24642031
UniProtP11712|CP2C9_HUMAN Cytochrome P450 2C9 (Gene Name=CYP2C9)

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