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7BX1

Crystal structure of RTT109 from Candida albicans

Functional Information from GO Data
ChainGOidnamespacecontents
A0004402molecular_functionhistone acetyltransferase activity
A0005634cellular_componentnucleus
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
A0006351biological_processDNA-templated transcription
A0006355biological_processregulation of DNA-templated transcription
A0006974biological_processDNA damage response
A0010484molecular_functionhistone H3 acetyltransferase activity
A0016740molecular_functiontransferase activity
A0030447biological_processfilamentous growth
A0032931molecular_functionhistone H3K56 acetyltransferase activity
A0036166biological_processphenotypic switching
A0044182biological_processfilamentous growth of a population of unicellular organisms
A0061733molecular_functionprotein-lysine-acetyltransferase activity
A1900239biological_processregulation of phenotypic switching
A1900429biological_processnegative regulation of filamentous growth of a population of unicellular organisms
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue ACM A 401
ChainResidue
AILE24
ALYS42
AARG44
AILE327
AHOH574
AHOH605

site_idAC2
Number of Residues5
Detailsbinding site for residue ACM A 402
ChainResidue
APRO262
AHOH508
ALYS42
ATYR64
ALEU260

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"Q07794","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q07794","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q07794","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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