Structure of PDB 1qzz Chain A Binding Site BS01

Receptor Information
>1qzz Chain A (length=340) Species: 1924 (Streptomyces purpurascens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LEPTDQDLDVLLKNLGNLVTPMALRVAATLRLVDHLLAGADTLAGLADRT
DTHPQALSRLVRHLTVVGVLEGGEKGRPLRPTRLGMLLADGHPAQQRAWL
DLNGAVSHADLAFTGLLDVVRTGRPAYAGRYGRPFWEDLSADVALADSFD
ALMSCDEDLAYEAPADAYDWSAVRHVLDVGGGNGGMLAAIALRAPHLRGT
LVELAGPAERARRRFADAGLADRVTVAEGDFFKPLPVTADVVLLSFVLLN
WSDEDALTILRGCVRALEPGGRLLVLDRADRFFSTLLDLRMLTFMGGRVR
TRDEVVDLAGSAGLALASERTSGSTTLPFDFSILEFTAVS
Ligand information
Ligand IDSAM
InChIInChI=1S/C15H22N6O5S/c1-27(3-2-7(16)15(24)25)4-8-10(22)11(23)14(26-8)21-6-20-9-12(17)18-5-19-13(9)21/h5-8,10-11,14,22-23H,2-4,16H2,1H3,(H2-,17,18,19,24,25)/t7-,8+,10+,11+,14+,27-/m0/s1
InChIKeyMEFKEPWMEQBLKI-FCKMPRQPSA-N
SMILES
SoftwareSMILES
CACTVS 3.341C[S@@+](CC[C@H](N)C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0C[S+](CCC(C(=O)[O-])N)CC1C(C(C(O1)n2cnc3c2ncnc3N)O)O
CACTVS 3.341C[S+](CC[CH](N)C([O-])=O)C[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0C[S@@+](CC[C@@H](C(=O)[O-])N)C[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)O
ACDLabs 10.04[O-]C(=O)C(N)CC[S+](C)CC3OC(n2cnc1c(ncnc12)N)C(O)C3O
FormulaC15 H22 N6 O5 S
NameS-ADENOSYLMETHIONINE
ChEMBLCHEMBL1235831
DrugBank
ZINC
PDB chain1qzz Chain A Residue 635 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1qzz Crystal Structure of Aclacinomycin-10-Hydroxylase, a S-Adenosyl-L-Methionine-dependent Methyltransferase Homolog Involved in Anthracycline Biosynthesis in Streptomyces purpurascens.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		W146 Y171 G190 G191 E213 L214 G239 D240 F241 S255 F256 N260 W261
Binding residue
(residue number reindexed from 1)		W136 Y161 G180 G181 E203 L204 G229 D230 F231 S245 F246 N250 W251
Annotation score1
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.-
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1qzz, PDBe:1qzz, PDBj:1qzz
PDBsum1qzz
PubMed14607118
UniProtQ54527|RDMB_STREF Aclacinomycin 10-hydroxylase RdmB (Gene Name=rdmB)

[Back to BioLiP]