Structure of PDB 4xnh Chain B Binding Site BS03

Receptor Information
>4xnh Chain B (length=197) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PINIRRATINDIICMQNANLHNLPENYMMKYYMYHILSWPEASFVATTTT
LDCEDRTIKLDPTYLAPGEKLVGYVLVKMNDDPNEPPNGHITSLSVMRTY
RRMGIAENLMRQALFALREVHQAEYVSLHVRQSNRAALHLYRDTLAFEVL
SIEKSYYQDGEDAYAMKKVLKLEELQISNFTHRREKLEDDLESDLLE
Ligand information
Ligand IDCMC
InChIInChI=1S/C23H38N7O18P3S/c1-23(2,18(35)21(36)26-4-3-13(31)25-5-6-52-8-14(32)33)9-45-51(42,43)48-50(40,41)44-7-12-17(47-49(37,38)39)16(34)22(46-12)30-11-29-15-19(24)27-10-28-20(15)30/h10-12,16-18,22,34-35H,3-9H2,1-2H3,(H,25,31)(H,26,36)(H,32,33)(H,40,41)(H,42,43)(H2,24,27,28)(H2,37,38,39)/t12-,16-,17-,18+,22-/m1/s1
InChIKeyOBUOSIHPWVNVJN-GRFIIANRSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=C(O)CSCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O
CACTVS 3.370CC(C)(CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23)[CH](O)C(=O)NCCC(=O)NCCSCC(O)=O
OpenEye OEToolkits 1.7.2CC(C)(COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)C(C(=O)NCCC(=O)NCCSCC(=O)O)O
OpenEye OEToolkits 1.7.2CC(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)[C@H](C(=O)NCCC(=O)NCCSCC(=O)O)O
CACTVS 3.370CC(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)[C@@H](O)C(=O)NCCC(=O)NCCSCC(O)=O
FormulaC23 H38 N7 O18 P3 S
NameCARBOXYMETHYL COENZYME *A
ChEMBL
DrugBank
ZINCZINC000085534448
PDB chain4xnh Chain F Residue 301 [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]
PDB4xnh Crystal structure of yeast N-terminal acetyltransferase NatE (IP6) in complex with a bisubstrate
Resolution2.1 Å
Binding residue
(original residue number in PDB)		L24 S117 L118 S119 V120 R125 R126 G128 A130 E131 H153 V154 A160 H163 Y165 T168 R207
Binding residue
(residue number reindexed from 1)		L23 S93 L94 S95 V96 R101 R102 G104 A106 E107 H129 V130 A136 H139 Y141 T144 R183
Annotation score3
Enzymatic activity
Enzyme Commision number 2.3.1.255: N-terminal amino-acid N(alpha)-acetyltransferase NatA.
Gene Ontology
Molecular Function
GO:0004596 peptide alpha-N-acetyltransferase activity
GO:0005515 protein binding
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0042802 identical protein binding
GO:1990189 peptide-serine-alpha-N-acetyltransferase activity
GO:1990190 peptide-glutamate-alpha-N-acetyltransferase activity
Biological Process
GO:0006474 N-terminal protein amino acid acetylation
Cellular Component
GO:0005737 cytoplasm
GO:0031415 NatA complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4xnh, PDBe:4xnh, PDBj:4xnh
PDBsum4xnh
PubMed
UniProtP07347|ARD1_YEAST N-terminal acetyltransferase A complex catalytic subunit ARD1 (Gene Name=ARD1)

[Back to BioLiP]