Structure of PDB 5ex9 Chain A

Receptor sequence
>5ex9A (length=414) Species: 55952 (Streptomyces toyocaensis) [Search protein sequence]
IPNPLLGLDSTENLYFQGIDPFTMFEEINVVRASQLHRRDRFDPVPELHS
LMKEGGLTVLGTEDSTEGRTAWLATGIDEVRQVLGSDKFSARLLYGGTAA
GITWPGFLTQYDPPEHTRLRRMVVPAFSHRRMQKFRPRVEQIVQDSLDTI
ESLGGPVDFVPHFGWAIATPATCDFLGIPRDDQADLARILLASRTDRSDK
RRTAAGNKFMTYMKQHVAQSRRGSGDDLFGIVGRENGDAITDAELTGVAA
FVMGAAADQVARLLAAGAWLMVEQPAQFALLREKPETVPEWLDETMRYLT
TDEKTHPRVATQDVRIGNQLVKAGDTVTCSLLAANRPNYPSAEDEFDITR
EKAEHLAFGHGIHHCLGRAMAELMFKVSIPALAHRFPTLRLADPQREITL
GPPPFDVEALLLDW
3D structure
PDB5ex9 Biochemical and structural characterisation of the second oxidative crosslinking step during the biosynthesis of the glycopeptide antibiotic A47934.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T172 A232 D235 Q236 V237 C342 L343 G344 M351 P381
Catalytic site (residue number reindexed from 1) T195 A255 D258 Q259 V260 C365 L366 G367 M374 P404
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 A L85 T86 H93 R97 F228 A233 V237 D279 T282 H283 R285 A334 F335 H340 C342 L343 G344 L108 T109 H116 R120 F251 A256 V260 D302 T305 H306 R308 A357 F358 H363 C365 L366 G367
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:5ex9, PDBe:5ex9, PDBj:5ex9
PDBsum5ex9
PubMed28144358
UniProtQ8KLL7

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