4PSX
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 |
D | 0004402 | molecular_function | histone acetyltransferase activity |
D | 0005634 | cellular_component | nucleus |
D | 0006325 | biological_process | chromatin organization |
D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
D | 0031509 | biological_process | subtelomeric heterochromatin formation |
D | 0042393 | molecular_function | histone binding |
E | 0000123 | cellular_component | histone acetyltransferase complex |
E | 0000781 | cellular_component | chromosome, telomeric region |
E | 0004402 | molecular_function | histone acetyltransferase activity |
E | 0005515 | molecular_function | protein binding |
E | 0005634 | cellular_component | nucleus |
E | 0005737 | cellular_component | cytoplasm |
E | 0006325 | biological_process | chromatin organization |
E | 0006338 | biological_process | chromatin remodeling |
E | 0006355 | biological_process | regulation of DNA-templated transcription |
E | 0031509 | biological_process | subtelomeric heterochromatin formation |
E | 0033698 | cellular_component | Rpd3L complex |
E | 0042393 | molecular_function | histone binding |
E | 0070210 | cellular_component | Rpd3L-Expanded complex |
F | 0000786 | cellular_component | nucleosome |
F | 0003677 | molecular_function | DNA binding |
F | 0030527 | molecular_function | structural constituent of chromatin |
F | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE COA A 401 |
Chain | Residue |
A | PHE160 |
A | SER233 |
A | ASN258 |
A | HOH565 |
A | HOH594 |
A | HOH596 |
C | LYS12 |
C | HOH118 |
A | ILE161 |
A | PHE220 |
A | ILE222 |
A | GLN227 |
A | ASN228 |
A | LYS229 |
A | GLY230 |
A | GLY232 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 501 |
Chain | Residue |
B | GLN41 |
B | ARG123 |
B | ARG125 |
B | SER167 |
B | PHE168 |
B | HOH610 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE COA D 401 |
Chain | Residue |
D | ILE161 |
D | PHE220 |
D | LEU221 |
D | ILE222 |
D | TYR226 |
D | GLN227 |
D | ASN228 |
D | GLY230 |
D | GLY232 |
D | SER233 |
D | ASN258 |
D | LEU264 |
D | ARG267 |
D | HOH530 |
D | HOH540 |
D | HOH595 |
D | HOH598 |
F | LYS12 |
F | HOH113 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_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 |
Chain | Residue | Details |
Y | LYS4 | |
P | LYS4 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:17194708 |
Chain | Residue | Details |
Y | LYS9 | |
P | LYS9 | |
C | LYS12 | |
F | LYS5 | |
F | LYS8 | |
F | LYS12 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:10911986, ECO:0000269|PubMed:10975519, ECO:0000269|PubMed:15719021 |
Chain | Residue | Details |
Y | SER10 | |
P | SER10 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-butyryllysine; alternate => ECO:0000269|PubMed:19113941, ECO:0000269|PubMed:27105113 |
Chain | Residue | Details |
Y | LYS14 | |
P | LYS14 |
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 |
site_id | MCSA2 |
Number of Residues | 2 |
Details | M-CSA 224 |
Chain | Residue | Details |
D | PHE220 | electrostatic stabiliser, hydrogen bond donor |
D | GLU255 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |