4PSW
Crystal structure of histone acetyltransferase complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004402 | molecular_function | histone acetyltransferase activity |
A | 0005634 | cellular_component | nucleus |
A | 0006325 | biological_process | chromatin organization |
A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
A | 0031509 | biological_process | subtelomeric heterochromatin formation |
A | 0042393 | molecular_function | histone binding |
B | 0000123 | cellular_component | histone acetyltransferase complex |
B | 0000781 | cellular_component | chromosome, telomeric region |
B | 0004402 | molecular_function | histone acetyltransferase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0006325 | biological_process | chromatin organization |
B | 0006338 | biological_process | chromatin remodeling |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0031509 | biological_process | subtelomeric heterochromatin formation |
B | 0033698 | cellular_component | Rpd3L complex |
B | 0042393 | molecular_function | histone binding |
B | 0070210 | cellular_component | Rpd3L-Expanded complex |
C | 0000786 | cellular_component | nucleosome |
C | 0003677 | molecular_function | DNA binding |
C | 0030527 | molecular_function | structural constituent of chromatin |
C | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE COA A 401 |
Chain | Residue |
A | SER218 |
A | ASN258 |
A | ARG267 |
A | HOH529 |
C | LYS14 |
A | PHE220 |
A | ILE222 |
A | GLN227 |
A | ASN228 |
A | LYS229 |
A | GLY230 |
A | GLY232 |
A | SER233 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | SITE: Important for interaction with HAT1 => ECO:0000269|PubMed:24835250 |
Chain | Residue | Details |
B | LEU266 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24835250, ECO:0000269|PubMed:9727486 |
Chain | Residue | Details |
A | PHE220 | |
A | GLN227 | |
A | ASN258 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9727486 |
Chain | Residue | Details |
A | ARG267 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Interaction with histone H4 N-terminus => ECO:0000269|PubMed:24835250 |
Chain | Residue | Details |
A | TRP174 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 224 |
Chain | Residue | Details |
A | PHE220 | electrostatic stabiliser, hydrogen bond donor |
A | GLU255 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |