Structure of PDB 5veu Chain H

Receptor sequence
>5veuH (length=459) Species: 9606 (Homo sapiens) [Search protein sequence]
TRTHGLFKRLGIPGPTPLPLLGNVLSYRQGLWKFDTECYKKYGKMWGTYE
GQLPVLAITDPDVIRTVLVKECYSVFTNRRSLGPVGFMKSAISLAEDEEW
KRIRSLLSPTFTSGKLKEMFPIIAQYGDVLVRNLRREAEKGKPVTLKDIF
GAYSMDVITGTSFGVNIDSLNNPQDPFVESTKKFLKFGFLDPLFLSIILF
PFLTPVFEALNVSLFPKDTINFLSKSVNRMKKSRLNDKQKHRLDFLQLMI
DSQNSALSDLELAAQSIIFIFAGYETTSSVLSFTLYELATHPDVQQKLQK
EIDAVLPNKAPPTYDAVVQMEYLDMVVNETLRLFPVAIRLERTCKKDVEI
NGVFIPKGSMVVIPTYALHHDPKYWTEPEEFRPERFSDSIDPYIYTPFGT
GPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLDTQGLLQPEK
PIVLKVDSR
3D structure
PDB5veu The X-Ray Crystal Structure of the Human Mono-Oxygenase Cytochrome P450 3A5-Ritonavir Complex Reveals Active Site Differences between P450s 3A4 and 3A5.
ChainH
Resolution2.91 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T309 F434 C441
Catalytic site (residue number reindexed from 1) T276 F398 C405
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 H R105 I118 R130 F302 A305 T309 V369 L373 R375 P433 F434 R439 C441 I442 R79 I92 R104 F269 A272 T276 V336 L340 R342 P397 F398 R403 C405 I406
BS02 RIT H R105 F210 F213 F220 L240 I301 F304 A305 T309 E374 G480 L481 R79 F184 F187 F194 L214 I268 F271 A272 T276 E341 G444 L445 BindingDB: Ki=120nM
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0008401 retinoic acid 4-hydroxylase 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:0019825 oxygen binding
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0050649 testosterone 6-beta-hydroxylase activity
GO:0070330 aromatase activity
GO:0101020 estrogen 16-alpha-hydroxylase activity
Biological Process
GO:0002933 lipid hydroxylation
GO:0006805 xenobiotic metabolic process
GO:0008202 steroid metabolic process
GO:0008210 estrogen metabolic process
GO:0009822 alkaloid catabolic process
GO:0042178 xenobiotic catabolic process
GO:0042572 retinol metabolic process
GO:0042573 retinoic acid metabolic process
GO:0046222 aflatoxin metabolic process
GO:0070989 oxidative demethylation
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum 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:5veu, PDBe:5veu, PDBj:5veu
PDBsum5veu
PubMed29093019
UniProtP20815|CP3A5_HUMAN Cytochrome P450 3A5 (Gene Name=CYP3A5)

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