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2P0W

Human histone acetyltransferase 1 (HAT1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004402molecular_functionhistone acetyltransferase activity
A0005634cellular_componentnucleus
A0006325biological_processchromatin organization
A0031509biological_processsubtelomeric heterochromatin formation
A0042393molecular_functionhistone binding
B0004402molecular_functionhistone acetyltransferase activity
B0005634cellular_componentnucleus
B0006325biological_processchromatin organization
B0031509biological_processsubtelomeric heterochromatin formation
B0042393molecular_functionhistone binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 805
ChainResidue
APHE247
AHOH932
AHOH1059
AHOH1139

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 806
ChainResidue
AALA275
AARG286
AHIS327
AHOH1023
AHOH1170

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE ACO A 401
ChainResidue
APHE185
ASER239
AMET241
ALEU242
AILE243
AGLN248
AGLY249
AGLN250
AGLY251
AHIS252
AGLY253
AALA254
APRO278
ASER279
ASER281
ATYR282
ALYS284
ALEU285
APHE288
AHOH828
AHOH900
AHOH930
AHOH1152
AHOH1173
AHOH1181

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ACO B 401
ChainResidue
BPHE185
BSER239
BMET241
BLEU242
BILE243
BGLN248
BGLY249
BGLN250
BGLY251
BGLY253
BALA254
BPRO278
BSER279
BSER281
BTYR282
BLYS284
BLEU285
BHOH842
BHOH969

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACM A 801
ChainResidue
AGLU97
AASN98
ACYS101
AHOH1127
BTYR162

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACM B 802
ChainResidue
AASN156
AASN209
BGLY18
BASP100
BCYS101
BHOH819

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACM A 803
ChainResidue
AGLY140
ACYS168
AHOH1093

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACM B 804
ChainResidue
BGLU24
BLYS26
BCYS27
BTYR69
BLYS70
BGLY71
BLEU72

Functional Information from PROSITE/UniProt
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
PGLY14-HIS18

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsRegion: {"description":"Interaction with histone H4 N-terminus","evidences":[{"source":"PubMed","id":"22615379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsRegion: {"description":"Interaction with histone H4 N-terminus","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"22615379","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22615379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Interaction with histone H4 N-terminus","evidences":[{"source":"PubMed","id":"22615379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by AMPK","evidences":[{"source":"PubMed","id":"28143904","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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