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1Z4R

Human GCN5 Acetyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004402molecular_functionhistone acetyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
Functional Information from PDB Data
site_idAC1
Number of Residues34
DetailsBINDING SITE FOR RESIDUE ACO A 401
ChainResidue
AHIS502
APHE578
ACYS579
AALA580
AVAL581
AGLN586
AVAL587
ALYS588
AGLY589
ATYR590
AGLY591
AALA512
ATHR592
ATHR612
ATYR613
AASP615
ATYR617
AGLY620
ATYR621
ALYS624
AHOH1002
AHOH1008
AASN513
AHOH1013
AHOH1024
AHOH1033
AHOH1036
AHOH1044
AARG515
ATRP519
AGLN530
ALEU531
AILE576
AVAL577

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:27796307, ECO:0000269|PubMed:31527837
ChainResidueDetails
AGLU575

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:29211711, ECO:0007744|PDB:5TRL
ChainResidueDetails
ACYS579
AGLN586
ATYR617

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:23142079
ChainResidueDetails
ALYS549

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ygh
ChainResidueDetails
AGLU575

site_idCSA2
Number of Residues9
DetailsAnnotated By Reference To The Literature 1ygh
ChainResidueDetails
AILE642
ALEU611
ATYR645
AGLU575
ACYS579
AILE576
AVAL577
APHE568
APHE573

site_idMCSA1
Number of Residues9
DetailsM-CSA 524
ChainResidueDetails
APHE568electrostatic stabiliser
APHE573electrostatic stabiliser
AGLU575proton acceptor
AILE576electrostatic stabiliser
AVAL577electrostatic stabiliser
ACYS579electrostatic stabiliser
ALEU611electrostatic stabiliser
AILE642electrostatic stabiliser
ATYR645electrostatic stabiliser

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PDB entries from 2024-10-09

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