Structure of PDB 6k3q Chain B Binding Site BS02

Receptor Information
>6k3q Chain B (length=453) Species: 1404 (Priestia megaterium) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYL
SSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENK
RQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDE
NIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPV
PSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDE
LMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIG
QQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKK
IPL
Ligand information
Ligand IDD0F
InChIInChI=1S/C23H32N2O4/c26-21(14-13-17-8-3-1-4-9-17)25-15-7-12-20(25)22(27)24-19(23(28)29)16-18-10-5-2-6-11-18/h2,5-6,10-11,17,19-20H,1,3-4,7-9,12-16H2,(H,24,27)(H,28,29)/t19-,20-/m0/s1
InChIKeyFYUKGHZWIUVSTO-PMACEKPBSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.7c1ccc(cc1)C[C@@H](C(=O)O)NC(=O)[C@@H]2CCCN2C(=O)CCC3CCCCC3
OpenEye OEToolkits 2.0.7c1ccc(cc1)CC(C(=O)O)NC(=O)C2CCCN2C(=O)CCC3CCCCC3
CACTVS 3.385OC(=O)[CH](Cc1ccccc1)NC(=O)[CH]2CCCN2C(=O)CCC3CCCCC3
CACTVS 3.385OC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H]2CCCN2C(=O)CCC3CCCCC3
FormulaC23 H32 N2 O4
Name(2S)-2-[[(2S)-1-(3-cyclohexylpropanoyl)pyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic acid;
N-(3-cyclohexylpropanoyl)-L-prolyl-L-phenylalanine
ChEMBL
DrugBank
ZINC
PDB chain6k3q Chain B Residue 503 [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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PDB6k3q Systematic Evolution of Decoy Molecules for the Highly Efficient Hydroxylation of Benzene and Small Alkanes Catalyzed by Wild-Type Cytochrome P450BM3
Resolution2.06 Å
Binding residue
(original residue number in PDB)		L20 F42 R47 Y51 S72 Q73 A74 A328 P329 A330 M354 L437
Binding residue
(residue number reindexed from 1)		L18 F40 R45 Y49 S70 Q71 A72 A326 P327 A328 M352 L435
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) T268 F393 C400
Catalytic site (residue number reindexed from 1) T266 F391 C398
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:6k3q, PDBe:6k3q, PDBj:6k3q
PDBsum6k3q
PubMed
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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