Structure of PDB 4lx9 Chain A Binding Site BS02

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 IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain4lx9 Chain A Residue 302 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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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)
H137 E176
Binding residue
(residue number reindexed from 1)
H78 E117
Annotation score1
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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