5ZQY
Crystal structure of a poly(ADP-ribose) glycohydrolase
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 401 |
| Chain | Residue |
| A | ASP314 |
| A | ASP316 |
| A | THR317 |
| A | AR6403 |
| A | HOH501 |
| A | HOH624 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | ASP316 |
| A | AR6403 |
| A | HOH501 |
| A | HOH648 |
| A | THR76 |
| A | ASP77 |
| A | ASP78 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | binding site for residue AR6 A 403 |
| Chain | Residue |
| A | ASP77 |
| A | GLY115 |
| A | GLY117 |
| A | ALA118 |
| A | GLY119 |
| A | VAL120 |
| A | PHE143 |
| A | GLY147 |
| A | SER148 |
| A | TYR149 |
| A | GLY150 |
| A | ASN151 |
| A | GLY152 |
| A | HIS182 |
| A | ILE271 |
| A | ASP314 |
| A | THR317 |
| A | MG401 |
| A | MG402 |
| A | HOH501 |
| A | HOH506 |
| A | HOH553 |
| A | HOH555 |
| A | HOH598 |
| A | HOH606 |
| A | HOH610 |
| A | HOH611 |
| A | HOH624 |
| A | HOH656 |
| A | HOH718 |
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 | GLU41 |
| 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 | THR76 |
| 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 | LYS146 | |
| A | HIS182 | |
| A | ASP77 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:34321462, ECO:0007744|PDB:7ARW |
| Chain | Residue | Details |
| A | ASP78 |
| 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 | ILE271 | |
| A | LEU235 |
| 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 | ASP316 | |
| A | ASP314 |
| 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 | THR317 |
| 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 | GLU41 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | THR64 |
