Structure of PDB 5veu Chain A

Receptor sequence
>5veuA (length=462) Species: 9606 (Homo sapiens) [Search protein sequence]
TRTHGLFKRLGIPGPTPLPLLGNVLSYRQGLWKFDTECYKKYGKMWGTYE
GQLPVLAITDPDVIRTVLVKECYSVFTNRRSLGPVGFMKSAISLAEDEEW
KRIRSLLSPTFTSGKLKEMFPIIAQYGDVLVRNLRREAEKGKPVTLKDIF
GAYSMDVITGTSFGVNIDSLNNPQDPFVESTKKFLKFGFLDPLFLSIILF
PFLTPVFEALNVSLFPKDTINFLSKSVNRMKKSRLNDKQKHRLDFLQLMI
DSQNSALSDLELAAQSIIFIFAGYETTSSVLSFTLYELATHPDVQQKLQK
EIDAVLPNKAPPTYDAVVQMEYLDMVVNETLRLFPVAIRLERTCKKDVEI
NGVFIPKGSMVVIPTYALHHDPKYWTEPEEFRPERFSKKKDSIDPYIYTP
FGTGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLDTQGLLQ
PEKPIVLKVDSR
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.
ChainA
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 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 R105 W126 R130 F302 A305 T309 L373 R375 P433 F434 G435 R439 C441 I442 A447 R79 W100 R104 F269 A272 T276 L340 R342 P400 F401 G402 R406 C408 I409 A414
BS02 RIT A F210 F213 F215 F241 I301 F304 T309 A370 G480 F184 F187 F189 F215 I268 F271 T276 A337 G447 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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