Structure of PDB 4h24 Chain D Binding Site BS01

Receptor Information
>4h24 Chain D (length=455) Species: 1404 (Priestia megaterium) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLS
SQRLIKEACDESRFDKNLSQALKFARDFAGDGLVTSWTHEKNWKKAHNIL
LPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVSEDMTRLTLDTI
GLCGFNYRFNSFYRDQPHPFIISMVRALDEVMNKLQRANPDDPAYDENKR
QFQEDIKVMNDLVDKIIADRKARGEQSDDLLTQMLNGKDPETGEPLDDGN
IRYQIITFLIAGHEATSGLLSFALYFLVKNPHVLQKVAEEAARVLVDPVP
SYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDEV
MVLIPQLHRDKTVWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQ
QFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPKGFVVKAKSKKI
PLGGI
Ligand information
Ligand IDHEM
InChIInChI=1S/C34H34N4O4.Fe/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;/h7-8,13-16H,1-2,9-12H2,3-6H3,(H4,35,36,37,38,39,40,41,42);/q;+2/p-2/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;
InChIKeyKABFMIBPWCXCRK-RGGAHWMASA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1c2n3c(c1CCC(=O)O)C=C4C(=C(C5=[N]4[Fe]36[N]7=C(C=C8N6C(=C5)C(=C8C)C=C)C(=C(C7=C2)C)C=C)C)CCC(=O)O
CACTVS 3.385CC1=C(CCC(O)=O)C2=Cc3n4[Fe]5|6|N2=C1C=c7n5c(=CC8=N|6C(=Cc4c(C)c3CCC(O)=O)C(=C8C=C)C)c(C)c7C=C
ACDLabs 12.01C=1c3c(c(c4C=C5C(=C(C=6C=C7C(=C(C8=CC=2C(=C(C=1N=2[Fe](n34)(N5=6)N78)CCC(=O)O)C)\C=C)C)\C=C)C)C)CCC(=O)O
FormulaC34 H32 Fe N4 O4
NamePROTOPORPHYRIN IX CONTAINING FE;
HEME
ChEMBL
DrugBankDB18267
ZINC
PDB chain4h24 Chain D Residue 500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4h24 A serine-substituted P450 catalyzes highly efficient carbene transfer to olefins in vivo.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		K69 L86 V87 F107 F261 A264 G265 A268 T269 F331 P392 F393 R398 C400 I401 G402 A406
Binding residue
(residue number reindexed from 1)		K66 L83 V84 F104 F258 A261 G262 A265 T266 F328 P389 F390 R395 C397 I398 G399 A403
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) A268 F393 C400
Catalytic site (residue number reindexed from 1) A265 F390 C397
Enzyme Commision number 1.14.14.1: unspecific monooxygenase.
1.6.2.4: NADPH--hemoprotein reductase.
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

View graph for
Molecular Function
External links
PDB RCSB:4h24, PDBe:4h24, PDBj:4h24
PDBsum4h24
PubMed23792734
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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