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2OZU

Crystal structure of human MYST histone acetyltransferase 3 in complex with acetylcoenzyme A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004402molecular_functionhistone acetyltransferase activity
A0006355biological_processregulation of DNA-templated transcription
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 800
ChainResidue
ACYS540
ACYS543
AHIS556
ACYS560

site_idAC2
Number of Residues31
DetailsBINDING SITE FOR RESIDUE ACO A 850
ChainResidue
AHOH36
AHOH70
AHOH86
ALYS516
ATYR517
AGLU518
ATRP522
APHE600
ALEU601
ASER645
AILE647
AMET648
AILE649
AGLN654
AARG655
ALYS656
AGLY657
AGLY659
AARG660
ALEU683
ASER684
ALEU686
ALEU689
ASER690
AALA693
AACM903
AHOH2
AHOH3
AHOH20
AHOH21
AHOH30

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACM A 901
ChainResidue
ALYS573
AHIS705
ACYS773

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACM A 902
ChainResidue
AGLU635
ACYS638
AGLN639
AGLN640
ATYR642

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACM A 903
ChainResidue
AALY604
ASER645
ACYS646
AACO850

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACM A 904
ChainResidue
AILE588
AGLN591
ACYS723
APRO724
AGLN725

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues25
DetailsZN_FING: C2HC MYST-type => ECO:0000255|PROSITE-ProRule:PRU01063
ChainResidueDetails
ALEU537-TRP562

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q9H7Z6
ChainResidueDetails
AGLU680

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|Ref.27
ChainResidueDetails
ASER645
AGLN654
ASER684

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|Ref.27
ChainResidueDetails
AALY604

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mj9
ChainResidueDetails
ACYS646
AGLU680

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PDB entries from 2024-10-30

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