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 | 168 |
| Details | Domain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Region: {"description":"Interaction with histone H4 N-terminus","evidences":[{"source":"PubMed","id":"24835250","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Region: {"description":"Interaction with HAT2","evidences":[{"source":"PubMed","id":"24835250","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8858151","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"24835250","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24835250","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9727486","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9727486","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Site: {"description":"Interaction with histone H4 N-terminus","evidences":[{"source":"PubMed","id":"24835250","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 31 |
| Details | Repeat: {"description":"WD 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 31 |
| Details | Repeat: {"description":"WD 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 31 |
| Details | Repeat: {"description":"WD 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 31 |
| Details | Repeat: {"description":"WD 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 31 |
| Details | Repeat: {"description":"WD 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 31 |
| Details | Repeat: {"description":"WD 6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | Region: {"description":"Interaction with the histone H4 N-terminus","evidences":[{"source":"PubMed","id":"24835250","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for interaction with HAT1","evidences":[{"source":"PubMed","id":"24835250","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 |
