Structure of PDB 5mnv Chain H

Receptor sequence
>5mnvH (length=395) Species: 1890 (Streptomyces antibioticus) [Search protein sequence]
AVPAYPFSLPHALDLDPHYAELRRDEPVSRVRLPYGEGTAWLVTRMSDAR
IVLGDSRFSTAAATDPATPRMFPTPPEPDGVLAQDPPDHTRLRRLVGKAF
TARRVEEMRPRVRSLVDSLLDDMVAHGSPADLVEFLAVPFPVAVICELLG
VPLEDRDLFRTFSDAMLSSTRLTAAEIQRVQQDFMVYMDGLVAQRRDAPT
EDLLGALALATDNDDHLTKGEIVNMGVSLLIAGHETSVNQITNLVHLLLT
ERKRYESLVADPALVPAAVEEMLRYTPLVSAGSFVRVATEDVELSTVTVR
AGEPCVVHFASANRDEEVFDHADELDFHRERNPHIAFGHGAHHCIGAQLG
RLELQEALSALVRRFPTLDLAEPVAGLKWKQGMLIRGLERQIVSW
3D structure
PDB5mnv Substrate-induced conformational change in cytochrome P450 OleP.
ChainH
Resolution2.97 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S180 A244 E247 T248 S249 S292 C356 I357 G358 E365 I397
Catalytic site (residue number reindexed from 1) S168 A232 E235 T236 S237 S280 C344 I345 G346 E353 I385
Enzyme Commision number ?
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 V93 L94 R105 L241 A244 G245 T248 Q252 R298 A348 F349 G350 H354 C356 I357 G358 V81 L82 R93 L229 A232 G233 T236 Q240 R286 A336 F337 G338 H342 C344 I345 G346
BS02 DEB H F84 A244 S295 L396 F72 A232 S283 L384
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:5mnv, PDBe:5mnv, PDBj:5mnv
PDBsum5mnv
PubMed30207799
UniProtQ59819

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