Structure of PDB 3sma Chain D Binding Site BS01

Receptor Information
>3sma Chain D (length=264) Species: 359131 (Streptomyces rubellomurinus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RELVTRDRLASDLAALGVRPGGVLLVHASLSALGWVCGGAQAVVLALQDA
VGKEGTLVMPTFSGDLSDPSTWRRPPVPEDWWPVIREQMPPFDPDLTPTR
GMGAVAECFRRAAGAVRSGHPQNSFAAWGAHAEQVVAEHGLTERLGRGSP
LEQVYRLDGQVLLLGCGFESNTSFHLAEYRTAYPGRRSHRRRVPVPEGDR
VRWVEQEDIVYFEEDFQTMGESCLTRTPGHSRGTVGEAAAVLYGQRAFVD
LACEWMTAHRDLAR
Ligand information
Ligand IDACO
InChIInChI=1S/C23H38N7O17P3S/c1-12(31)51-7-6-25-14(32)4-5-26-21(35)18(34)23(2,3)9-44-50(41,42)47-49(39,40)43-8-13-17(46-48(36,37)38)16(33)22(45-13)30-11-29-15-19(24)27-10-28-20(15)30/h10-11,13,16-18,22,33-34H,4-9H2,1-3H3,(H,25,32)(H,26,35)(H,39,40)(H,41,42)(H2,24,27,28)(H2,36,37,38)/t13-,16-,17-,18+,22-/m1/s1
InChIKeyZSLZBFCDCINBPY-ZSJPKINUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)O
CACTVS 3.341CC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)CO[P@@](O)(=O)O[P@](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O[P](O)(O)=O)n2cnc3c(N)ncnc23
ACDLabs 10.04O=C(SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O)C
CACTVS 3.341CC(=O)SCCNC(=O)CCNC(=O)[CH](O)C(C)(C)CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0CC(=O)SCCNC(=O)CCNC(=O)C(C(C)(C)COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)O
FormulaC23 H38 N7 O17 P3 S
NameACETYL COENZYME *A
ChEMBLCHEMBL1230809
DrugBank
ZINCZINC000008551095
PDB chain3sma Chain D Residue 300 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3sma New N-Acetyltransferase Fold in the Structure and Mechanism of the Phosphonate Biosynthetic Enzyme FrbF.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		R19 H45 A46 S47 L48 S49 V54 F80 G121 A122 S188 T190 H193 E231
Binding residue
(residue number reindexed from 1)		R1 H27 A28 S29 L30 S31 V36 F62 G103 A104 S170 T172 H175 E213
Annotation score4
Enzymatic activity
Enzyme Commision number 2.3.1.-
Gene Ontology
Molecular Function
GO:0008080 N-acetyltransferase activity
GO:0016746 acyltransferase activity
GO:0046353 aminoglycoside 3-N-acetyltransferase activity
Biological Process
GO:0017000 antibiotic biosynthetic process
GO:0046677 response to antibiotic

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3sma, PDBe:3sma, PDBj:3sma
PDBsum3sma
PubMed21865168
UniProtQ0ZQ43|FRBF_STRR3 CMP-5'-(N-hydroxy-3-aminopropyl)phosphonate acetyltransferase (Gene Name=frbF)

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