Structure of PDB 3kx3 Chain A Binding Site BS02

Receptor Information
>3kx3 Chain A (length=454) Species: 1404 (Priestia megaterium) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYL
SSQRLIKEACDESRFDKNLSQALKFVRDFAGDGEFTSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENK
RQFQEDIKVMNDLVDKIIADRKASQSDDLLTHMLNGKDPETGEPLDDENI
RYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPS
YKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELM
VLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQ
FALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIP
LGGI
Ligand information
Ligand ID140
InChIInChI=1S/C18H35NO3/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-17(20)19-16-18(21)22/h2-16H2,1H3,(H,19,20)(H,21,22)
InChIKeyKVTFEOAKFFQCCX-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(NCC(=O)O)CCCCCCCCCCCCCCC
OpenEye OEToolkits 1.5.0CCCCCCCCCCCCCCCC(=O)NCC(=O)O
CACTVS 3.341CCCCCCCCCCCCCCCC(=O)NCC(O)=O
FormulaC18 H35 N O3
NameN-PALMITOYLGLYCINE;
N-HEXADECANOYLGLYCINE
ChEMBLCHEMBL226117
DrugBankDB03440
ZINCZINC000008689962
PDB chain3kx3 Chain A Residue 1470 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3kx3 Glutamate-haem ester bond formation is disfavoured in flavocytochrome P450 BM3: characterization of glutamate substitution mutants at the haem site of P450 BM3.
Resolution1.803 Å
Binding residue
(original residue number in PDB)		Y51 S72 Q73 A74 F87 L188
Binding residue
(residue number reindexed from 1)		Y49 S70 Q71 A72 F85 L186
Annotation score1
Binding affinityBindingDB: Kd=82nM
Enzymatic activity
Catalytic site (original residue number in PDB) T268 F393 C400
Catalytic site (residue number reindexed from 1) T264 F389 C396
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:3kx3, PDBe:3kx3, PDBj:3kx3
PDBsum3kx3
PubMed20180779
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

[Back to BioLiP]