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3TO9

Crystal structure of yeast Esa1 E338Q HAT domain bound to coenzyme A with active site lysine acetylated

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 Residues22
DetailsBINDING SITE FOR RESIDUE COA A 500
ChainResidue
AHOH4
ACYS304
AILE305
ALEU306
ATHR307
AGLN312
AARG313
AMET314
AGLY315
AGLY317
ALYS318
AHOH8
ASER342
ALEU344
ASER348
AHOH21
AHOH68
AHOH79
AHOH96
AHOH102
APHE258
ALEU259

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 506
ChainResidue
AARG245
AARG249
ATYR266
AEDO501

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 507
ChainResidue
AGLN203
ATYR204
AASN250

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 508
ChainResidue
AARG230
AHIS284
ATYR397
ALYS398

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 509
ChainResidue
AGLN400
AHIS401

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 501
ChainResidue
AHOH59
AARG245
AEDO506

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CAD A 502
ChainResidue
AALY262
ATHR263
APHE271
AHOH479

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues25
DetailsZinc finger: {"description":"C2HC MYST-type; degenerate","evidences":[{"source":"PROSITE-ProRule","id":"PRU01063","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"12368900","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"17223684","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"18245364","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000303"},{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11106757","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12368900","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 525
ChainResidueDetails
ALEU308covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
ASER342activator, proton acceptor, proton donor

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PDB entries from 2025-12-10

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