Structure of PDB 4lx9 Chain A Binding Site BS01

Receptor Information
>4lx9 Chain A (length=157) Species: 273057 (Saccharolobus solfataricus P2) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DFTLRNARMDDIDQIIKINRLTLPENYPYYFFVEHLKEYGLAFFVAIVDN
SVVGYIMPRIEWGFSNIKQLPSLVRKGHVVSIAVLEEYRRKGIATTLLEA
SMKSMKNDYNAEEIYLEVRVSNYPAIALYEKLNFKKVKVLKGYYADGEDA
YLMARPL
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 chain4lx9 Chain A Residue 301 [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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PDB4lx9 Implications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal ortholog.
Resolution1.98 Å
Binding residue
(original residue number in PDB)		L82 I141 V143 R148 R149 G151 A153 T154 E176 P183 L187 Y188 K190
Binding residue
(residue number reindexed from 1)		L23 I82 V84 R89 R90 G92 A94 T95 E117 P124 L128 Y129 K131
Annotation score4
Enzymatic activity
Enzyme Commision number 2.3.1.255: N-terminal amino-acid N(alpha)-acetyltransferase NatA.
2.3.1.258: N-terminal methionine N(alpha)-acetyltransferase NatE.
Gene Ontology
Molecular Function
GO:0004596 peptide alpha-N-acetyltransferase activity
GO:0008080 N-acetyltransferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0046872 metal ion binding
GO:0120518 peptide-methionine-alpha-N-acetyltransferase activity
Biological Process
GO:0006474 N-terminal protein amino acid acetylation
Cellular Component
GO:0005737 cytoplasm
GO:0031415 NatA complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4lx9, PDBe:4lx9, PDBj:4lx9
PDBsum4lx9
PubMed23959863
UniProtQ980R9|NAT_SACS2 N-alpha-acetyltransferase (Gene Name=ard1)

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