7S68
Structure of human PARP1 domains (Zn1, Zn3, WGR and HD) bound to a DNA double strand break.
Functional Information from GO Data
Functional Information from PROSITE/UniProt
| site_id | PS00347 |
| Number of Residues | 36 |
| Details | ZF_PARP_1 Zinc finger poly(ADP-ribose) polymerase (PARP)-type signature. CKkCsesIpKdslRmaimvqspmfdgkvph..WYHfsC |
| Chain | Residue | Details |
| A | CYS21-CYS56 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 84 |
| Details | ZN_FING: PARP-type 1 => ECO:0000255|PROSITE-ProRule:PRU00264 |
| Chain | Residue | Details |
| A | TYR9-GLY203 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 90 |
| Details | ZN_FING: PARP-type 2 => ECO:0000255|PROSITE-ProRule:PRU00264 |
| Chain | Residue | Details |
| A | LYS223-GLY313 | |
| B | LYS621 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:21233213, ECO:0000269|PubMed:22582261, ECO:0000269|PubMed:22683995, ECO:0007744|PDB:3OD8, ECO:0007744|PDB:3ODA, ECO:0007744|PDB:4AV1, ECO:0007744|PDB:4DQY, ECO:0007744|PDB:4OPX, ECO:0007744|PDB:4OQA, ECO:0007744|PDB:4OQB |
| Chain | Residue | Details |
| A | CYS21 | |
| A | CYS24 | |
| A | HIS53 | |
| A | CYS56 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:21233213, ECO:0000269|PubMed:22683995, ECO:0007744|PDB:3ODC, ECO:0007744|PDB:3ODE, ECO:0007744|PDB:4AV1 |
| Chain | Residue | Details |
| A | GLU235 | |
| A | LEU238 | |
| A | LYS269 | |
| A | VAL272 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01351, ECO:0000269|PubMed:18055453, ECO:0000269|PubMed:22582261, ECO:0007744|PDB:2RIQ, ECO:0007744|PDB:4DQY, ECO:0007744|PDB:4OPX, ECO:0007744|PDB:4OQA, ECO:0007744|PDB:4OQB |
| Chain | Residue | Details |
| A | CYS295 | |
| A | CYS298 | |
| A | CYS311 | |
| A | CYS321 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | SITE: Cleavage; by caspase-3 and caspase-7 => ECO:0000269|PubMed:10497198, ECO:0000269|PubMed:22464733, ECO:0000269|PubMed:7596430 |
| Chain | Residue | Details |
| A | ASP214 | |
| B | ALA762 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|Ref.12, ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | ALA2 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER41 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS207 | |
| A | GLY215 | |
| A | GLN241 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | MET287 | |
| A | CYS295 | |
| A | SER274 | |
| A | SER277 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | PHE289 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER364 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 3 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| A | LEU302 | |
| A | LYS249 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| A | GLY313 |
