6TX3
HPF1 bound to catalytic fragment of PARP2
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+ poly-ADP-ribosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue UHB B 1001 |
| Chain | Residue |
| B | HIS415 |
| B | TYR442 |
| B | TYR449 |
| B | SER457 |
| B | TYR460 |
| B | GLU545 |
| B | GLY416 |
| B | SER417 |
| B | ASN421 |
| B | GLY424 |
| B | ILE425 |
| B | GLY429 |
| B | ARG431 |
| B | PRO434 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 227 |
| Details | Domain: {"description":"PARP catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00397","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"For poly [ADP-ribose] polymerase activity","evidences":[{"source":"PubMed","id":"26704974","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"30104678","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"32028527","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"32028527","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6TX3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"32028527","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33589610","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33683197","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"PolyADP-ribosyl aspartic acid","evidences":[{"source":"PubMed","id":"33589610","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"ADP-ribosyltyrosine","evidences":[{"source":"PubMed","id":"29954836","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30257210","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"PolyADP-ribosyl glutamic acid","evidences":[{"source":"PubMed","id":"33589610","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
