Structure of PDB 1izo Chain A

Receptor sequence
>1izoA (length=411) Species: 1423 (Bacillus subtilis) [Search protein sequence]
PHDKSLDNSLTLLKEGYLFIKNRTERYNSDLFQARLLGKNFICMTGAEAA
KVFYDTDRFQRQNALPKRVQKSLFGVNAIQGMDGSAHIHRKMLFLSLMTP
PHQKRLAELMTEEWKAAVTRWEKADEVVLFEEAKEILCRVACYWAGVPLK
ETEVKERADDFIDMVDAFGAVGPRHWKGRRARPRAEEWIEVMIEDARAGL
LKTTSGTALHEMAFHTQEDGSQLDSRMAAIELINVLRPIVAISYFLVFSA
LALHEHPKYKEWLRSGNSREREMFVQEVRRYYPFGPFLGALVKKDFVWNN
CEFKKGTSVLLDLYGTNHDPRLWDHPDEFRPERFAEREENLFDMIPQGGG
HAEKGHRCPGEGITIEVMKASLDFLVHQIEYDVPEQSLHYSLARMPSLPE
SGFVMSGIRRK
3D structure
PDB1izo Substrate Recognition and Molecular Mechanism of Fatty Acid Hydroxylation by Cytochrome P450 from Bacillus subtilis. CRYSTALLOGRAPHIC, SPECTROSCOPIC, AND MUTATIONAL STUDIES.
ChainA
Resolution2.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.11.2.4: fatty-acid peroxygenase.
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 Y59 R66 H92 K96 F99 M103 P243 A246 I247 F250 F289 L293 Q352 H361 C363 P364 G365 Y54 R61 H87 K91 F94 M98 P238 A241 I242 F245 F284 L288 Q347 H356 C358 P359 G360
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:0020037 heme binding
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:1izo, PDBe:1izo, PDBj:1izo
PDBsum1izo
PubMed12519760
UniProtO31440|CYPC_BACSU Fatty-acid peroxygenase (Gene Name=cypC)

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