Structure of PDB 6js8 Chain A Binding Site BS02

Receptor Information

>6js8 Chain A (length=455) Species: 1404 (Priestia megaterium)

TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTR
YLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAH
NILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTL
DTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDE
NKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLD
DENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVD
PVPSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKG
DELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKS
KKIPL

Ligand information

• Ligand ID: C5R
• InChI: InChI=1S/C31H38N2O3/c1-19(2)20-10-12-24-21(16-20)11-13-27-30(24,3)14-7-15-31(27,4)29(36)33-26(28(34)35)17-22-18-32-25-9-6-5-8-23(22)25/h5-6,8-10,12,16,18-19,26-27,32H,7,11,13-15,17H2,1-4H3,(H,33,36)(H,34,35)/t26-,27+,30+,31+/m0/s1
• InChIKey: WYAQKAIGBDDJPR-QKOWHPQASA-N
• SMILES:
  OpenEye OEToolkits 2.0.6: CC(C)c1ccc2c(c1)CCC3C2(CCCC3(C)C(=O)NC(Cc4c[nH]c5c4cccc5)C(=O)O)C
  OpenEye OEToolkits 2.0.6: CC(C)c1ccc2c(c1)CC[C@@H]3[C@@]2(CCC[C@@]3(C)C(=O)N[C@@H](Cc4c[nH]c5c4cccc5)C(=O)O)C
  CACTVS 3.385: CC(C)c1ccc2c(CC[CH]3[C](C)(CCC[C]23C)C(=O)N[CH](Cc4c[nH]c5ccccc45)C(O)=O)c1
  CACTVS 3.385: CC(C)c1ccc2c(CC[C@H]3[C@@](C)(CCC[C@]23C)C(=O)N[C@@H](Cc4c[nH]c5ccccc45)C(O)=O)c1
• Formula: C31 H38 N2 O3
• Name: (2S)-2-[[(1R,4aS,10aR)-1,4a-dimethyl-7-propan-2-yl-2,3,4,9,10,10a-hexahydrophenanthren-1-yl]carbonylamino]-3-(1H-indol-3-yl)propanoic acid;
  N-Dehydroabietoyl-L-Tryptophan
• PDB chain: 6js8 Chain A Residue 503

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6js8 Crystals in Minutes: Instant On-Site Microcrystallisation of Various Flavours of the CYP102A1 (P450BM3) Haem Domain.
• Resolution: 1.36 Å
• Binding residue (original residue number in PDB): R47 Y51 S72 Q73 A74 F87 M185 L188 L437
• Binding residue (residue number reindexed from 1): R47 Y51 S72 Q73 A74 F87 M185 L188 L437
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): T268 F393 C400
• Catalytic site (residue number reindexed from 1): T268 F393 C400
• 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

External links

• PDB: RCSB:6js8, PDBe:6js8, PDBj:6js8
• PDBsum: 6js8
• PubMed: 32157795
• UniProt: P14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)