Structure of PDB 1r00 Chain A

Receptor sequence
>1r00A (length=340) Species: 1924 (Streptomyces purpurascens) [Search protein sequence]
LEPTDQDLDVLLKNLGNLVTPMALRVAATLRLVDHLLAGADTLAGLADRT
DTHPQALSRLVRHLTVVGVLEGGEKGRPLRPTRLGMLLADGHPAQQRAWL
DLNGAVSHADLAFTGLLDVVRTGRPAYAGRYGRPFWEDLSADVALADSFD
ALMSCDEDLAYEAPADAYDWSAVRHVLDVGGGNGGMLAAIALRAPHLRGT
LVELAGPAERARRRFADAGLADRVTVAEGDFFKPLPVTADVVLLSFVLLN
WSDEDALTILRGCVRALEPGGRLLVLDRADRFFSTLLDLRMLTFMGGRVR
TRDEVVDLAGSAGLALASERTSGSTTLPFDFSILEFTAVS
3D structure
PDB1r00 Crystal Structure of Aclacinomycin-10-Hydroxylase, a S-Adenosyl-L-Methionine-dependent Methyltransferase Homolog Involved in Anthracycline Biosynthesis in Streptomyces purpurascens.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L259 N260 D287 V316
Catalytic site (residue number reindexed from 1) L249 N250 D277 V299
Enzyme Commision number 4.1.1.-
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 SAH A W146 Y171 G190 G191 E213 L214 P217 G239 D240 F241 S255 W261 W136 Y161 G180 G181 E203 L204 P207 G229 D230 F231 S245 W251
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008171 O-methyltransferase activity
GO:0016829 lyase activity
GO:0016831 carboxy-lyase activity
Biological Process
GO:0017000 antibiotic biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1r00, PDBe:1r00, PDBj:1r00
PDBsum1r00
PubMed14607118
UniProtQ54527|RDMB_STREF Aclacinomycin 10-hydroxylase RdmB (Gene Name=rdmB)

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