2G4K
Anomalous substructure of human ADP-ribosylhydrolase 3
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0004649 | molecular_function | poly(ADP-ribose) glycohydrolase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005694 | cellular_component | chromosome |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006281 | biological_process | DNA repair |
| A | 0006287 | biological_process | base-excision repair, gap-filling |
| A | 0016604 | cellular_component | nuclear body |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0060546 | biological_process | negative regulation of necroptotic process |
| A | 0061463 | molecular_function | O-acetyl-ADP-ribose deacetylase activity |
| A | 0071451 | biological_process | cellular response to superoxide |
| A | 0090734 | cellular_component | site of DNA damage |
| A | 0140290 | biological_process | peptidyl-serine ADP-deribosylation |
| A | 0140292 | molecular_function | ADP-ribosylserine hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 351 |
| Chain | Residue |
| A | THR60 |
| A | ASP61 |
| A | ASP62 |
| A | ASP300 |
| A | HOH355 |
| A | HOH357 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 352 |
| Chain | Residue |
| A | THR301 |
| A | HOH355 |
| A | HOH356 |
| A | GLU25 |
| A | ASP298 |
| A | ASP300 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 353 |
| Chain | Residue |
| A | GLN211 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 354 |
| Chain | Residue |
| A | SER5 |
| A | ARG8 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21892188, ECO:0000269|PubMed:29907568, ECO:0000269|PubMed:30045870, ECO:0007744|PDB:5ZQY, ECO:0007744|PDB:6D36, ECO:0007744|PDB:6D3A |
| Chain | Residue | Details |
| A | GLU25 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21892188, ECO:0000269|PubMed:29907568, ECO:0000269|PubMed:30045870, ECO:0000269|PubMed:33894202, ECO:0007744|PDB:5ZQY, ECO:0007744|PDB:6D36, ECO:0007744|PDB:6D3A, ECO:0007744|PDB:7L9I |
| Chain | Residue | Details |
| A | THR60 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29907568, ECO:0000269|PubMed:30045870, ECO:0007744|PDB:5ZQY, ECO:0007744|PDB:6D36, ECO:0007744|PDB:6D3A |
| Chain | Residue | Details |
| A | ASP61 | |
| A | LYS130 | |
| A | HIS166 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:34321462, ECO:0007744|PDB:7ARW |
| Chain | Residue | Details |
| A | ASP62 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29907568, ECO:0007744|PDB:6D36, ECO:0007744|PDB:6D3A |
| Chain | Residue | Details |
| A | LEU219 | |
| A | ILE255 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21892188, ECO:0000269|PubMed:29907568, ECO:0000269|PubMed:30045870, ECO:0000269|PubMed:33894202, ECO:0000269|PubMed:34321462, ECO:0007744|PDB:5ZQY, ECO:0007744|PDB:6D36, ECO:0007744|PDB:6D3A, ECO:0007744|PDB:7AKR, ECO:0007744|PDB:7AKS, ECO:0007744|PDB:7ARW, ECO:0007744|PDB:7L9H |
| Chain | Residue | Details |
| A | ASP298 | |
| A | ASP300 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21892188, ECO:0000269|PubMed:29907568, ECO:0000269|PubMed:30045870, ECO:0000269|PubMed:33894202, ECO:0007744|PDB:5ZQY, ECO:0007744|PDB:6D36, ECO:0007744|PDB:6D3A, ECO:0007744|PDB:7L9H |
| Chain | Residue | Details |
| A | THR301 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | SITE: Glutamate flap => ECO:0000269|PubMed:29907568, ECO:0000269|PubMed:30045870 |
| Chain | Residue | Details |
| A | GLU25 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | THR48 |
