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9MJG

Crystal structure of HAT1 in complex with XS380871

This is a non-PDB format compatible entry.
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
C0004402molecular_functionhistone acetyltransferase activity
C0005634cellular_componentnucleus
C0006325biological_processchromatin organization
C0031509biological_processsubtelomeric heterochromatin formation
C0042393molecular_functionhistone binding
D0004402molecular_functionhistone acetyltransferase activity
D0005634cellular_componentnucleus
D0006325biological_processchromatin organization
D0031509biological_processsubtelomeric heterochromatin formation
D0042393molecular_functionhistone binding
E0004402molecular_functionhistone acetyltransferase activity
E0005634cellular_componentnucleus
E0006325biological_processchromatin organization
E0031509biological_processsubtelomeric heterochromatin formation
E0042393molecular_functionhistone binding
F0004402molecular_functionhistone acetyltransferase activity
F0005634cellular_componentnucleus
F0006325biological_processchromatin organization
F0031509biological_processsubtelomeric heterochromatin formation
F0042393molecular_functionhistone binding
G0004402molecular_functionhistone acetyltransferase activity
G0005634cellular_componentnucleus
G0006325biological_processchromatin organization
G0031509biological_processsubtelomeric heterochromatin formation
G0042393molecular_functionhistone binding
H0004402molecular_functionhistone acetyltransferase activity
H0005634cellular_componentnucleus
H0006325biological_processchromatin organization
H0031509biological_processsubtelomeric heterochromatin formation
H0042393molecular_functionhistone binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues16
DetailsRegion: {"description":"Interaction with histone H4 N-terminus","evidences":[{"source":"PubMed","id":"22615379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsRegion: {"description":"Interaction with histone H4 N-terminus","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"22615379","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsSite: {"description":"Interaction with histone H4 N-terminus","evidences":[{"source":"PubMed","id":"22615379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues64
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22615379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
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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