Structure of PDB 1zo4 Chain A

Receptor sequence

>1zo4A (length=456) Species: 1404 (Priestia megaterium)

TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTR
YLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAH
NILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTL
DTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDE
NKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLD
DENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVD
PVPSYKQVKQLKYVGMVLNEALRLWPTSPAFSLYAKEDTVLGGEYPLEKG
DELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRAC
IGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKS
KKIPLG

3D structure

• PDB: 1zo4 A single active-site mutation of P450BM-3 dramatically enhances substrate binding and rate of product formation.
• Chain: A
• Resolution: 1.46 Å

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.

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 F87 W96 A264 G265 T268 T269 F331 P392 F393 R398 C400 I401 G402 A406	K69 L86 F87 W96 A264 G265 T268 T269 F331 P392 F393 R398 C400 I401 G402 A406

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:1zo4, PDBe:1zo4, PDBj:1zo4
• PDBsum: 1zo4
• PubMed: 21875028
• UniProt: P14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)