Structure of PDB 5b2w Chain B

Receptor sequence

>5b2wB (length=452) Species: 1404 (Priestia megaterium)

EMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLS
SQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNIL
LPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTI
GLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKR
QFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDEN
IRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVP
SYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDEL
MVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQ
QFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKI
PL

3D structure

• PDB: 5b2w Crystal Structure of P450BM3 with decoy molecules
• Chain: B
• Resolution: 1.65 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T268 F393 C400
• Catalytic site (residue number reindexed from 1): T265 F390 C397
• 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 F261 A264 G265 T268 F331 P392 F393 R398 C400 I401 A406	K66 L83 F84 W93 F258 A261 G262 T265 F328 P389 F390 R395 C397 I398 A403
BS02	W1Z	B	L17 L20 A44 R47 Y51 S72 Q73 A74 L75 F87 L188 A264 A328 A330 L437 T438	L14 L17 A41 R44 Y48 S69 Q70 A71 L72 F84 L185 A261 A325 A327 L434 T435

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:5b2w, PDBe:5b2w, PDBj:5b2w
• PDBsum: 5b2w
• UniProt: P14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)