6M3I
Crystal structure of HPF1/PARP1 complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000785 | cellular_component | chromatin |
| A | 0003682 | molecular_function | chromatin binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005694 | cellular_component | chromosome |
| A | 0006281 | biological_process | DNA repair |
| A | 0006302 | biological_process | double-strand break repair |
| A | 0006974 | biological_process | DNA damage response |
| A | 0010835 | biological_process | regulation of protein ADP-ribosylation |
| A | 0042393 | molecular_function | histone binding |
| A | 0072572 | molecular_function | poly-ADP-D-ribose binding |
| A | 0090734 | cellular_component | site of DNA damage |
| A | 0140768 | molecular_function | protein ADP-ribosyltransferase-substrate adaptor activity |
| A | 0140861 | biological_process | DNA repair-dependent chromatin remodeling |
| B | 0003950 | molecular_function | NAD+-protein poly-ADP-ribosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue UNU B 1101 |
| Chain | Residue |
| B | HIS862 |
| B | GLY863 |
| B | TYR896 |
| B | PHE897 |
| B | SER904 |
| B | TYR907 |
| B | GLU988 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: For poly [ADP-ribose] polymerase activity => ECO:0000305|PubMed:32028527, ECO:0000305|PubMed:7852410, ECO:0000305|PubMed:9315851 |
| Chain | Residue | Details |
| B | GLU988 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9UGN5 |
| Chain | Residue | Details |
| B | HIS862 | |
| B | GLY871 | |
| B | ARG878 | |
| B | SER904 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8CFE2 |
| Chain | Residue | Details |
| A | LYS19 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: ADP-ribosylserine => ECO:0000269|PubMed:30257210 |
| Chain | Residue | Details |
| A | SER97 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS186 | |
| A | LYS233 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: PolyADP-ribosyl aspartic acid => ECO:0000269|PubMed:33589610 |
| Chain | Residue | Details |
| A | ASP235 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: ADP-ribosyltyrosine => ECO:0000269|PubMed:29954836, ECO:0000269|PubMed:30257210 |
| Chain | Residue | Details |
| A | TYR238 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000269|PubMed:33589610 |
| Chain | Residue | Details |
| A | GLU240 |
