Structure of PDB 5ex6 Chain B

Receptor sequence
>5ex6B (length=371) Species: 55952 (Streptomyces toyocaensis) [Search protein sequence]
RPPIHTLRQGFDPADELRAAGELTRVRLEHTWLATGHDVVRQVLGDHTRF
STRRRFLVGNLMDYDPPEHTRLRRLLAPGFTHRKIRRMAPYIEQIVTERL
DEMEREGSPADLIELFADEVPGPVLCELLGVPRDDRAMFLQLCHRHLDAS
LSGRRRAAAGEAFSRYLVTMVARERKDPGDGLIGMVVAEHGDTVTDEELR
GVCVQMMLAGDDNISGMIGLGVLALLRNPEQIAALRGDVPAAERAVDELI
RYLTVPYAPTPRTAIEDSTVGDQVIKAGETVLCSLPTANRDPALLPDADR
LDVTREAVPHVAFGHGVHHCLGAALARLELRIAYTALWRRFPDLRLADPD
GATEFRLSTPAYGISRLMVTW
3D structure
PDB5ex6 More than just recruitment: the X-domain influences catalysis of the first phenolic coupling reaction in A47934 biosynthesis by Cytochrome P450 StaH.
ChainB
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D175 A236 D239 N240 I241 C347 L348 G349 E356 A388
Catalytic site (residue number reindexed from 1) D148 A209 D212 N213 I214 C320 L321 G322 E329 A361
Enzyme Commision number ?
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 L88 H96 R100 M233 A236 G237 N240 P283 P286 T287 R289 A339 F340 H345 C347 G349 L61 H69 R73 M206 A209 G210 N213 P256 P259 T260 R262 A312 F313 H318 C320 G322
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
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:5ex6, PDBe:5ex6, PDBj:5ex6
PDBsum5ex6
PubMed27477788
UniProtQ8KLL9

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