Structure of PDB 2ij2 Chain B

Receptor sequence

>2ij2B (length=448) Species: 1404 (Priestia megaterium)

MPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSS
QRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNILL
PSFSQQAMKGYHAMMVDIAVQLVQKWERLNAEHIEVPEDMTRLTLDTIGL
CGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRYDENKRQFQEDIKVM
NDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIRYQIITFL
IAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLK
YVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHR
DKTIWGDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATLV
LGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPLGGIPSP

3D structure

• PDB: 2ij2 Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets. New heme ligation states influence conformational equilibria in P450 BM3.
• Chain: B
• Resolution: 1.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T268 F393 C400
• Catalytic site (residue number reindexed from 1): T256 F380 C387
• 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	B	K69 L86 F87 W96 A264 G265 T268 T269 F331 P392 F393 R398 C400 I401 G402 A406	K65 L82 F83 W92 A252 G253 T256 T257 F319 P379 F380 R385 C387 I388 G389 A393

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:2ij2, PDBe:2ij2, PDBj:2ij2
• PDBsum: 2ij2
• PubMed: 17077084
• UniProt: P14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)