Structure of PDB 6b11 Chain B

Receptor sequence
>6b11B (length=383) Species: 1906 (Streptomyces fradiae) [Search protein sequence]
SIAWPVARTCPFSPPEQYAALRAEEPIARAELWDGAPVWLISRQDHVRAL
LADPRVSIHPAKLPRLSPSDGEAEASRSLLTLDPPDHGALRGHFIPEFGL
RRVRELRPSVEQIVTGLLDDLTARGDEADLLADFALPMATQVICRLLDIP
YEDRDYFQERTEQATRPAAGEEALEALLELRDYLDRLISGKDGMLGSMVA
QARGGGLSHADVLDNAVLLLAAGHETTASMVTMSVLVLLQHPTAWRELTV
NPGLLPGAVDELLRYLSIADGLRRSATADIEIDGHTIRAGDGLVFLLAAA
NRDEAVFSEPEAFDIHRSARRHVAFGYGPHQCLGQNLARMELEVALGAVL
ERLPALRPTTDVAGLRLKSDSAVFGVYELPVAW
3D structure
PDB6b11 TylHI in complex with native substrate 23-deoxy-5-O-mycaminosyl-tylonolide (23-DMTL)
ChainB
Resolution1.99 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R197 E262 T263 C369 L370 G371
Catalytic site (residue number reindexed from 1) R166 E225 T226 C332 L333 G334
Enzyme Commision number 1.14.15.34: 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase.
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 L110 L111 H118 R122 F129 G260 T263 L309 R311 A361 F362 H367 C369 G371 A375 L79 L80 H87 R91 F98 G223 T226 L272 R274 A324 F325 H330 C332 G334 A338
BS02 CGM B G102 E103 E105 A195 P198 A204 L205 V254 L255 A258 A409 G71 E72 E74 A164 P167 A173 L174 V217 L218 A221 A372
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
Biological Process
GO:0016999 antibiotic metabolic process
GO:0017000 antibiotic biosynthetic process

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Molecular Function

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Biological Process
External links
PDB RCSB:6b11, PDBe:6b11, PDBj:6b11
PDBsum6b11
PubMed
UniProtQ9ZHQ1|TYLH1_STRFR 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase (Gene Name=tylH1)

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