Structure of PDB 7y0p Chain A

Receptor sequence

>7y0pA (length=451) Species: 1348623 (Priestia megaterium NBRC 15308 = ATCC 14581)

KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYL
SSQRLIKEACDESRFDKNLSQALKFVRDFTGDGLATSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRPDDPAYDENKRQ
FQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENI
RYQIITFLLAGHEVTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPS
YKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELM
VLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQ
FALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIP
L

3D structure

• PDB: 7y0p Crystal structure of the P450 BM3 heme domain mutant F87A/T268V/A82T/I263L in complex with N-imidazolyl-hexanoyl-L-phenylalanine, p-cresol and hydroxylamine
• Chain: A
• Resolution: 1.99 Å

Enzymatic activity

• Enzyme Commision number: 1.14.14.1: unspecific monooxygenase.
  1.6.2.4: NADPH--hemoprotein reductase.

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	A	K69 L86 A87 W96 I153 F261 A264 V268 T269 F331 P392 F393 G394 R398 C400 I401 G402 A406	K67 L84 A85 W94 I151 F257 A260 V264 T265 F327 P388 F389 G390 R394 C396 I397 G398 A402
BS02	HOA	A	A264 V268	A260 V264
BS03	PCR	A	L181 L263 A264 E267 V268	L179 L259 A260 E263 V264
BS04	IC6	A	P25 Y51 L188 A328 A330 L437	P23 Y49 L186 A324 A326 L433
BS05	IC6	A	L20 F42 R47 Y51 S72 Q73 A74 A328	L18 F40 R45 Y49 S70 Q71 A72 A324
BS06	PCR	A	Y160 V216 I219	Y158 V212 I215

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:7y0p, PDBe:7y0p, PDBj:7y0p
• PDBsum: 7y0p
• UniProt: P14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)