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1FY7

CRYSTAL STRUCTURE OF YEAST ESA1 HISTONE ACETYLTRANSFERASE DOMAIN COMPLEXED WITH COENZYME A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004402molecular_functionhistone acetyltransferase activity
A0006355biological_processregulation of DNA-templated transcription
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 1
ChainResidue
AALA303
ACOA500

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE COA A 500
ChainResidue
AGLN312
AARG313
AMET314
AGLY315
AGLY317
ALYS318
ALEU341
ASER342
ALEU344
AGLY345
ASER348
AARG421
AHOH502
AHOH505
AHOH597
ANA1
ATRP180
APHE258
ALEU259
AILE305
ALEU306
ATHR307

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues25
DetailsZN_FING: C2HC MYST-type; degenerate => ECO:0000255|PROSITE-ProRule:PRU01063
ChainResidueDetails
AILE195-LEU220

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000303|PubMed:12368900, ECO:0000303|PubMed:17223684, ECO:0000303|PubMed:18245364, ECO:0000303|PubMed:22020126, ECO:0000305
ChainResidueDetails
AGLU338

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11106757, ECO:0000269|PubMed:12368900, ECO:0000269|PubMed:22020126
ChainResidueDetails
AALA303
AGLN312
ASER342

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000305
ChainResidueDetails
ACYS304

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:22020126
ChainResidueDetails
ALYS262

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mj9
ChainResidueDetails
AGLU338
ACYS304

site_idMCSA1
Number of Residues2
DetailsM-CSA 525
ChainResidueDetails
ACYS304covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
AGLU338activator, proton acceptor, proton donor

219140

PDB entries from 2024-05-01

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