Structure of PDB 1qzz Chain A

Receptor sequence
>1qzzA (length=340) Species: 1924 (Streptomyces purpurascens) [Search protein sequence]
LEPTDQDLDVLLKNLGNLVTPMALRVAATLRLVDHLLAGADTLAGLADRT
DTHPQALSRLVRHLTVVGVLEGGEKGRPLRPTRLGMLLADGHPAQQRAWL
DLNGAVSHADLAFTGLLDVVRTGRPAYAGRYGRPFWEDLSADVALADSFD
ALMSCDEDLAYEAPADAYDWSAVRHVLDVGGGNGGMLAAIALRAPHLRGT
LVELAGPAERARRRFADAGLADRVTVAEGDFFKPLPVTADVVLLSFVLLN
WSDEDALTILRGCVRALEPGGRLLVLDRADRFFSTLLDLRMLTFMGGRVR
TRDEVVDLAGSAGLALASERTSGSTTLPFDFSILEFTAVS
3D structure
PDB1qzz Crystal Structure of Aclacinomycin-10-Hydroxylase, a S-Adenosyl-L-Methionine-dependent Methyltransferase Homolog Involved in Anthracycline Biosynthesis in Streptomyces purpurascens.
ChainA
Resolution2.1 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 SAM A W146 Y171 G190 G191 E213 L214 G239 D240 F241 S255 F256 N260 W261 W136 Y161 G180 G181 E203 L204 G229 D230 F231 S245 F246 N250 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:1qzz, PDBe:1qzz, PDBj:1qzz
PDBsum1qzz
PubMed14607118
UniProtQ54527|RDMB_STREF Aclacinomycin 10-hydroxylase RdmB (Gene Name=rdmB)

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