Structure of PDB 8ho0 Chain A

Receptor sequence
>8ho0A (length=391) Species: 1463854 (Streptomyces sp. NRRL F-5053) [Search protein sequence]
TLTYPFHDWSQELSPRYAQLRASDAPVCPVVSEGTGDPLWLVTRYATAVK
LLEDSRFSSEAAQASGAPRQSPVELRAPGTRGDAIAMLREAGLRSVLADG
LGPRAVRRHQGWINDLAETLMSELASREGTFDLAADFVEPLSSALVSRTL
LGELSADERDLLAHCADTGLRFCGVTHEEQVHAFTQMHEFFLEHARRLAG
TPGEHLLKLIAEAPLSDEALAEAGSLLVVAGFPTSSGFLCGALLTLLRHP
DAVQELHAHPERVPSAVEELLRYTPLSTGSVKRMATEDLEIDGVRIKAGE
VVMVSLEAVNHDPDAFEDPDVFRPGREGPMHFGFGRGRHFCPGNRLARCV
IEATVRAVARRPGLRLAVAPEEISWHEGLFFRRPRAIPATW
3D structure
PDB8ho0 Engineering the Substrate Specificity of a P450 Dimerase Enables the Collective Biosynthesis of Heterodimeric Tryptophan-Containing Diketopiperazines.
ChainA
Resolution1.71 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.-.-
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 A237 G238 F245 L283 V288 R290 G340 F341 H346 C348 P349 G350 A230 G231 F238 L276 V281 R283 G333 F334 H339 C341 P342 G343
BS02 3ZI A Q72 S284 G286 S287 V288 K289 L313 F387 F388 Q70 S277 G279 S280 V281 K282 L306 F380 F381
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0008395 steroid hydroxylase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0036199 cholest-4-en-3-one 26-monooxygenase activity
GO:0046872 metal ion binding
Biological Process
GO:0006707 cholesterol catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:8ho0, PDBe:8ho0, PDBj:8ho0
PDBsum8ho0
PubMed37083030
UniProtA0A8I3B027

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