Structure of PDB 7ydl Chain B

Receptor sequence
>7ydlB (length=452) Species: 1348623 (Priestia megaterium NBRC 15308 = ATCC 14581) [Search protein sequence]
EMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLS
SQRLIKEACDESRFDKNLSQALKFVRDFTGDGLATSWTHEKNWKKAHNIL
LPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTI
GLCGFNYRFNSFYRDQPHPFITSMVRALDEVMNKLQRANPDDPAYDENKR
QFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDEN
IRYQIITFLIAGHEITSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVP
SYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDEL
MVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQ
QFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKI
PL
3D structure
PDB7ydl Crystal structure of the P450 BM3 heme domain mutant F87A/T268I/A184V/A82T in complex with N-imidazolyl-hexanoyl-L-phenylalanine
ChainB
Resolution1.58 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
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 A87 W96 F261 A264 T269 F331 P392 F393 R398 C400 I401 G402 K66 L83 A84 W93 F258 A261 T266 F328 P389 F390 R395 C397 I398 G399
BS02 IC6 B S72 V78 A264 I268 A328 A330 L437 S69 V75 A261 I265 A325 A327 L434
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

View graph for
Molecular Function
External links
PDB RCSB:7ydl, PDBe:7ydl, PDBj:7ydl
PDBsum7ydl
PubMed
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

[Back to BioLiP]