Structure of PDB 1mja Chain A

Receptor sequence
>1mjaA (length=273) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
ARVRNLNRIIMGKYEIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKKQY
ERYRKKCTLRHPPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLSKLFLDH
KTLYYDVDPFLFYCMTRRDELGHHLVGYFSKEKESADGYNVACILTLPQY
QRMGYGKLLIEFSYELSKKENKVGSPEKPLSDLGLLSYRAYWSDTLITLL
VEHQKEITIDEISSMTSMTTTDILHTAKTLNILRYYKGQHIIFLNEDILD
RYNRLKAKKRRTIDPNRLIWKPP
3D structure
PDB1mja The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate.
ChainA
Resolution2.26 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C304 E338
Catalytic site (residue number reindexed from 1) C143 E177
Enzyme Commision number 2.3.1.-
2.3.1.48: histone acetyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 COA A F258 L259 C304 I305 L306 T307 Q312 R313 M314 G315 G317 K318 L341 S342 G345 R421 F97 L98 C143 I144 L145 T146 Q151 R152 M153 G154 G156 K157 L180 S181 G184 R260
Gene Ontology
Molecular Function
GO:0004402 histone acetyltransferase activity
Biological Process
GO:0006355 regulation of DNA-templated transcription

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Molecular Function
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Biological Process
External links
PDB RCSB:1mja, PDBe:1mja, PDBj:1mja
PDBsum1mja
PubMed12368900
UniProtQ08649|ESA1_YEAST Histone acetyltransferase ESA1 (Gene Name=ESA1)

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