Structure of PDB 5veu Chain D

Receptor sequence
>5veuD (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.
ChainD
Resolution2.91 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) 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 D R105 S119 W126 R130 F137 A305 T309 L373 R375 P433 F434 R439 C441 I442 A447 R79 S93 W100 R104 F111 A272 T276 L340 R342 P397 F398 R403 C405 I406 A411
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5veu, PDBe:5veu, PDBj:5veu
PDBsum5veu
PubMed29093019
UniProtP20815|CP3A5_HUMAN Cytochrome P450 3A5 (Gene Name=CYP3A5)

[Back to BioLiP]