7ARW
Structure of human ARH3 E41A bound to alpha-NAD+ and magnesium
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 |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0004649 | molecular_function | poly(ADP-ribose) glycohydrolase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005694 | cellular_component | chromosome |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0006281 | biological_process | DNA repair |
B | 0006287 | biological_process | base-excision repair, gap-filling |
B | 0016604 | cellular_component | nuclear body |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
B | 0046872 | molecular_function | metal ion binding |
B | 0060546 | biological_process | negative regulation of necroptotic process |
B | 0061463 | molecular_function | O-acetyl-ADP-ribose deacetylase activity |
B | 0071451 | biological_process | cellular response to superoxide |
B | 0090734 | cellular_component | site of DNA damage |
B | 0140290 | biological_process | peptidyl-serine ADP-deribosylation |
B | 0140292 | molecular_function | ADP-ribosylserine hydrolase activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
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 | ALA41 | |
B | ALA41 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
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 | |
B | THR76 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
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 | ASP77 | |
A | LYS146 | |
A | HIS182 | |
B | ASP77 | |
B | LYS146 | |
B | HIS182 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:34321462, ECO:0007744|PDB:7ARW |
Chain | Residue | Details |
A | ASP78 | |
B | ASP78 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:29907568, ECO:0007744|PDB:6D36, ECO:0007744|PDB:6D3A |
Chain | Residue | Details |
A | LEU235 | |
A | ILE271 | |
B | LEU235 | |
B | ILE271 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
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 | ASP314 | |
A | ASP316 | |
B | ASP314 | |
B | ASP316 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
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 | |
B | THR317 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | SITE: Glutamate flap => ECO:0000269|PubMed:29907568, ECO:0000269|PubMed:30045870 |
Chain | Residue | Details |
A | ALA41 | |
B | ALA41 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR64 | |
B | THR64 |