Structure of PDB 4dql Chain B

Receptor sequence

>4dqlB (length=379) Species: 1404 (Priestia megaterium)

KMHGAFSTNVVASKELQQPGSARSTRHLEIELPKEASYQEGDHLGVIPRN
YEGIVNRVTARFGLDASQQIRLKTVSVEELLQYVELQDPVTRTQLRAMAA
KTVCPPHKVELEALLEKQAYKEQVLAKRLTMLELLEKYPACEMKFSEFIA
LLPSIRPRYYSISSSPRVDEKQASITVSVVSGEAWSGYGEYKGIASNYLA
ELQEGDTITCFISTPQSEFTLPKDPETPLIMVGPGTGVAPFRGFVQARKQ
LKEQGQSLGEAHLYFGCRSPHEDYLYQEELENAQSEGIITLHTAFSRMPN
QPKTYVQHVMEQDGKKLIELLDQGAHFYICGDGSQMAPAVEATLMKSYAD
VHQVSEADARLWLQQLEEKGRYAKDVWAG

3D structure

• PDB: 4dql The crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3.
• Chain: B
• Resolution: 2.15 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y830 S831 C1000 D1045 W1047
• Catalytic site (residue number reindexed from 1): Y160 S161 C330 D375 W377
• 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	FAD	B	H700 R798 R828 Y829 Y830 S831 T846 E853 A854 W855 Y861 G863 I864 A865 S866 W1047 G1049	H43 R128 R158 Y159 Y160 S161 T176 E183 A184 W185 Y191 G193 I194 A195 S196 W377 G379
BS02	NAP	B	R680 G905 T906 C937 S966 R967 K973 Y975 Q977 M1006	R23 G235 T236 C267 S296 R297 K303 Y305 Q307 M336

Gene Ontology

Molecular Function

• GO:0016491 oxidoreductase activity

External links

• PDB: RCSB:4dql, PDBe:4dql, PDBj:4dql
• PDBsum: 4dql
• PubMed: 22356131
• UniProt: P14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)