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5J9T

Crystal structure of the NuA4 core complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004402molecular_functionhistone acetyltransferase activity
A0006355biological_processregulation of DNA-templated transcription
B0000123cellular_componenthistone acetyltransferase complex
B0004402molecular_functionhistone acetyltransferase activity
B0005634cellular_componentnucleus
B0006281biological_processDNA repair
B0006325biological_processchromatin organization
B0006338biological_processchromatin remodeling
B0006351biological_processDNA-templated transcription
B0033100cellular_componentNuA3 histone acetyltransferase complex
B0035267cellular_componentNuA4 histone acetyltransferase complex
B1990467cellular_componentNuA3a histone acetyltransferase complex
B1990468cellular_componentNuA3b histone acetyltransferase complex
C0006357biological_processregulation of transcription by RNA polymerase II
C0035267cellular_componentNuA4 histone acetyltransferase complex
E0004402molecular_functionhistone acetyltransferase activity
E0006355biological_processregulation of DNA-templated transcription
F0000123cellular_componenthistone acetyltransferase complex
F0004402molecular_functionhistone acetyltransferase activity
F0005634cellular_componentnucleus
F0006281biological_processDNA repair
F0006325biological_processchromatin organization
F0006338biological_processchromatin remodeling
F0006351biological_processDNA-templated transcription
F0033100cellular_componentNuA3 histone acetyltransferase complex
F0035267cellular_componentNuA4 histone acetyltransferase complex
F1990467cellular_componentNuA3a histone acetyltransferase complex
F1990468cellular_componentNuA3b histone acetyltransferase complex
G0006357biological_processregulation of transcription by RNA polymerase II
G0035267cellular_componentNuA4 histone acetyltransferase complex
I0004402molecular_functionhistone acetyltransferase activity
I0006355biological_processregulation of DNA-templated transcription
J0000123cellular_componenthistone acetyltransferase complex
J0004402molecular_functionhistone acetyltransferase activity
J0005634cellular_componentnucleus
J0006281biological_processDNA repair
J0006325biological_processchromatin organization
J0006338biological_processchromatin remodeling
J0006351biological_processDNA-templated transcription
J0033100cellular_componentNuA3 histone acetyltransferase complex
J0035267cellular_componentNuA4 histone acetyltransferase complex
J1990467cellular_componentNuA3a histone acetyltransferase complex
J1990468cellular_componentNuA3b histone acetyltransferase complex
K0006357biological_processregulation of transcription by RNA polymerase II
K0035267cellular_componentNuA4 histone acetyltransferase complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues75
DetailsZN_FING: C2HC MYST-type; degenerate => ECO:0000255|PROSITE-ProRule:PRU01063
ChainResidueDetails
EILE195-LEU220
AILE195-LEU220
IILE195-LEU220

site_idSWS_FT_FI2
Number of Residues3
DetailsACT_SITE: Proton donor/acceptor => ECO:0000303|PubMed:12368900, ECO:0000303|PubMed:17223684, ECO:0000303|PubMed:18245364, ECO:0000303|PubMed:22020126, ECO:0000305
ChainResidueDetails
EGLN338
AGLN338
IGLN338

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:11106757, ECO:0000269|PubMed:12368900, ECO:0000269|PubMed:22020126
ChainResidueDetails
EALA303
EGLN312
ESER342
AALA303
AGLN312
ASER342
IALA303
IGLN312
ISER342

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Important for catalytic activity => ECO:0000305
ChainResidueDetails
ECYS304
ACYS304
ICYS304

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:22020126
ChainResidueDetails
EALY262
AALY262
IALY262

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 525
ChainResidueDetails
ECYS304covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
EGLN338activator, proton acceptor, proton donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 525
ChainResidueDetails
ACYS304covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
AGLN338activator, proton acceptor, proton donor

site_idMCSA3
Number of Residues2
DetailsM-CSA 525
ChainResidueDetails
ICYS304covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
IGLN338activator, proton acceptor, proton donor

229380

PDB entries from 2024-12-25

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