Structure of PDB 1smi Chain A

Receptor sequence

>1smiA (length=439) Species: 1404 (Priestia megaterium)

TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTR
YLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAH
NILLPSFQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLD
TIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANQFQEDIKVM
NDLVDKIIADRKADDLLTHMLNGKDPETGEPLDDENIRYQIITFLIEGHE
TTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMV
LNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIW
GDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATLVLGMM
LKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPLG

3D structure

• PDB: 1smi A Single Mutation in Cytochrome P450 BM3 Induces the Conformational Rearrangement Seen upon Substrate Binding in the Wild-type Enzyme
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T268 F393 C400
• Catalytic site (residue number reindexed from 1): T251 F376 C383
• 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 F261 E264 G265 T268 F331 P392 F393 G394 R398 C400 I401 G402 A406	K69 L86 F87 W96 F244 E247 G248 T251 F314 P375 F376 G377 R381 C383 I384 G385 A389

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:1smi, PDBe:1smi, PDBj:1smi
• PDBsum: 1smi
• PubMed: 15020590
• UniProt: P14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)