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4PSX

Crystal structure of histone acetyltransferase complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004402molecular_functionhistone acetyltransferase activity
A0005634cellular_componentnucleus
A0006325biological_processchromatin organization
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0031509biological_processsubtelomeric heterochromatin formation
A0042393molecular_functionhistone binding
B0000123cellular_componenthistone acetyltransferase complex
B0000781cellular_componentchromosome, telomeric region
B0004402molecular_functionhistone acetyltransferase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006325biological_processchromatin organization
B0006338biological_processchromatin remodeling
B0006355biological_processregulation of DNA-templated transcription
B0031509biological_processsubtelomeric heterochromatin formation
B0033698cellular_componentRpd3L complex
B0042393molecular_functionhistone binding
B0070210cellular_componentRpd3L-Expanded complex
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0030527molecular_functionstructural constituent of chromatin
C0046982molecular_functionprotein heterodimerization activity
D0004402molecular_functionhistone acetyltransferase activity
D0005634cellular_componentnucleus
D0006325biological_processchromatin organization
D0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
D0031509biological_processsubtelomeric heterochromatin formation
D0042393molecular_functionhistone binding
E0000123cellular_componenthistone acetyltransferase complex
E0000781cellular_componentchromosome, telomeric region
E0004402molecular_functionhistone acetyltransferase activity
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0006325biological_processchromatin organization
E0006338biological_processchromatin remodeling
E0006355biological_processregulation of DNA-templated transcription
E0031509biological_processsubtelomeric heterochromatin formation
E0033698cellular_componentRpd3L complex
E0042393molecular_functionhistone binding
E0070210cellular_componentRpd3L-Expanded complex
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0030527molecular_functionstructural constituent of chromatin
F0046982molecular_functionprotein heterodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE COA A 401
ChainResidue
APHE160
ASER233
AASN258
AHOH565
AHOH594
AHOH596
CLYS12
CHOH118
AILE161
APHE220
AILE222
AGLN227
AASN228
ALYS229
AGLY230
AGLY232

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
BGLN41
BARG123
BARG125
BSER167
BPHE168
BHOH610

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE COA D 401
ChainResidue
DILE161
DPHE220
DLEU221
DILE222
DTYR226
DGLN227
DASN228
DGLY230
DGLY232
DSER233
DASN258
DLEU264
DARG267
DHOH530
DHOH540
DHOH595
DHOH598
FLYS12
FHOH113

Functional Information from PROSITE/UniProt
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
CGLY14-HIS18

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSGsdDhTVALWEV
ChainResidueDetails
BLEU176-VAL190
BVAL311-LEU325

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:11742990, ECO:0000269|PubMed:11751634, ECO:0000269|PubMed:11752412, ECO:0000269|PubMed:12152067, ECO:0000269|PubMed:12353038, ECO:0000269|PubMed:12845608, ECO:0000269|PubMed:15949446, ECO:0000269|PubMed:16122352, ECO:0000269|PubMed:16168379, ECO:0000269|PubMed:16185711, ECO:0000269|PubMed:17194708
ChainResidueDetails
YLYS4
PLYS4

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:17194708
ChainResidueDetails
YLYS9
PLYS9
CLYS12
FLYS5
FLYS8
FLYS12

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:10911986, ECO:0000269|PubMed:10975519, ECO:0000269|PubMed:15719021
ChainResidueDetails
YSER10
PSER10

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-butyryllysine; alternate => ECO:0000269|PubMed:19113941, ECO:0000269|PubMed:27105113
ChainResidueDetails
YLYS14
PLYS14

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 224
ChainResidueDetails
APHE220electrostatic stabiliser, hydrogen bond donor
AGLU255hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 224
ChainResidueDetails
DPHE220electrostatic stabiliser, hydrogen bond donor
DGLU255hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

219515

PDB entries from 2024-05-08

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