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9DZN

KAT6A MYST domain complexed with a H3K14-CoA bisubstrate inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004402molecular_functionhistone acetyltransferase activity
A0006355biological_processregulation of DNA-templated transcription
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0030527molecular_functionstructural constituent of chromatin
Functional Information from PROSITE/UniProt
site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
CLYS14-LEU20

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5","evidences":[{"source":"UniProtKB","id":"P68432","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PKC","evidences":[{"source":"UniProtKB","id":"P68431","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P68431","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Citrulline; alternate","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues25
DetailsZinc finger: {"description":"C2HC MYST-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01063","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"Q9H7Z6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"The crystal structure of human MYST histone acetyltransferase 3 in complex with acetylcoenzyme A.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"The crystal structure of human MYST histone acetyltransferase 3 in complex with acetylcoenzyme A.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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