Structure of PDB 1mjb Chain A

Receptor sequence
>1mjbA (length=273) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
ARVRNLNRIIMGKYEIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKKQY
ERYRKKCTLRHPPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLSKLFLDH
KTLYYDVDPFLFYCMTRRDELGHHLVGYFSKEKESADGYNVACILTLPQY
QRMGYGKLLIEFSYELSKKENKVGSPQKPLSDLGLLSYRAYWSDTLITLL
VEHQKEITIDEISSMTSMTTTDILHTAKTLNILRYYKGQHIIFLNEDILD
RYNRLKAKKRRTIDPNRLIWKPP
3D structure
PDB1mjb The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate.
ChainA
Resolution2.5 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 Q338
Catalytic site (residue number reindexed from 1) C143 Q177
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 ACO A W180 F258 L259 A303 C304 L306 T307 Q312 R313 M314 G315 S342 L344 G345 R421 W19 F97 L98 A142 C143 L145 T146 Q151 R152 M153 G154 S181 L183 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:1mjb, PDBe:1mjb, PDBj:1mjb
PDBsum1mjb
PubMed12368900
UniProtQ08649|ESA1_YEAST Histone acetyltransferase ESA1 (Gene Name=ESA1)

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