Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4PSW

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
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE COA A 401
ChainResidue
ASER218
AASN258
AARG267
AHOH529
CLYS14
APHE220
AILE222
AGLN227
AASN228
ALYS229
AGLY230
AGLY232
ASER233

Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSGsdDhTVALWEV
ChainResidueDetails
BLEU176-VAL190
BVAL311-LEU325

site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
CGLY16-HIS20

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Important for interaction with HAT1 => ECO:0000269|PubMed:24835250
ChainResidueDetails
BLEU266

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:24835250, ECO:0000269|PubMed:9727486
ChainResidueDetails
APHE220
AGLN227
AASN258

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:9727486
ChainResidueDetails
AARG267

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Interaction with histone H4 N-terminus => ECO:0000269|PubMed:24835250
ChainResidueDetails
ATRP174

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

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon