Structure of PDB 4lx9 Chain A Binding Site BS02
Receptor Information
>4lx9 Chain A (length=157) Species:
273057
(Saccharolobus solfataricus P2) [
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DFTLRNARMDDIDQIIKINRLTLPENYPYYFFVEHLKEYGLAFFVAIVDN
SVVGYIMPRIEWGFSNIKQLPSLVRKGHVVSIAVLEEYRRKGIATTLLEA
SMKSMKNDYNAEEIYLEVRVSNYPAIALYEKLNFKKVKVLKGYYADGEDA
YLMARPL
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
4lx9 Chain A Residue 302 [
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Receptor-Ligand Complex Structure
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PDB
4lx9
Implications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal ortholog.
Resolution
1.98 Å
Binding residue
(original residue number in PDB)
H137 E176
Binding residue
(residue number reindexed from 1)
H78 E117
Annotation score
1
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
PDBsum
4lx9
PubMed
23959863
UniProt
Q980R9
|NAT_SACS2 N-alpha-acetyltransferase (Gene Name=ard1)
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