6D36
Structure of human ARH3 bound to ADP-ribose 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 |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0004649 | molecular_function | poly(ADP-ribose) glycohydrolase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005654 | cellular_component | nucleoplasm |
| C | 0005694 | cellular_component | chromosome |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005759 | cellular_component | mitochondrial matrix |
| C | 0006281 | biological_process | DNA repair |
| C | 0006287 | biological_process | base-excision repair, gap-filling |
| C | 0016604 | cellular_component | nuclear body |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0060546 | biological_process | negative regulation of necroptotic process |
| C | 0061463 | molecular_function | O-acetyl-ADP-ribose deacetylase activity |
| C | 0071451 | biological_process | cellular response to superoxide |
| C | 0090734 | cellular_component | site of DNA damage |
| C | 0140290 | biological_process | peptidyl-serine ADP-deribosylation |
| C | 0140292 | molecular_function | ADP-ribosylserine hydrolase activity |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0004649 | molecular_function | poly(ADP-ribose) glycohydrolase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005654 | cellular_component | nucleoplasm |
| D | 0005694 | cellular_component | chromosome |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005759 | cellular_component | mitochondrial matrix |
| D | 0006281 | biological_process | DNA repair |
| D | 0006287 | biological_process | base-excision repair, gap-filling |
| D | 0016604 | cellular_component | nuclear body |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0060546 | biological_process | negative regulation of necroptotic process |
| D | 0061463 | molecular_function | O-acetyl-ADP-ribose deacetylase activity |
| D | 0071451 | biological_process | cellular response to superoxide |
| D | 0090734 | cellular_component | site of DNA damage |
| D | 0140290 | biological_process | peptidyl-serine ADP-deribosylation |
| D | 0140292 | molecular_function | ADP-ribosylserine hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue AR6 C 401 |
| Chain | Residue |
| C | ASP77 |
| C | TYR149 |
| C | GLY150 |
| C | ASN151 |
| C | GLY152 |
| C | HIS182 |
| C | ILE271 |
| C | ASP314 |
| C | THR317 |
| C | MG402 |
| C | MG403 |
| C | GLY115 |
| C | HOH502 |
| C | HOH519 |
| C | HOH554 |
| C | HOH570 |
| C | HOH595 |
| C | HOH745 |
| C | GLY117 |
| C | ALA118 |
| C | GLY119 |
| C | VAL120 |
| C | PHE143 |
| C | GLY147 |
| C | SER148 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue MG C 402 |
| Chain | Residue |
| C | ASP314 |
| C | ASP316 |
| C | THR317 |
| C | AR6401 |
| C | MG403 |
| C | HOH502 |
| C | HOH519 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue MG C 403 |
| Chain | Residue |
| C | THR76 |
| C | ASP77 |
| C | ASP78 |
| C | ASP316 |
| C | AR6401 |
| C | MG402 |
| C | HOH502 |
| C | HOH583 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | binding site for residue AR6 D 401 |
| Chain | Residue |
| D | ASP77 |
| D | GLY115 |
| D | GLY117 |
| D | ALA118 |
| D | GLY119 |
| D | VAL120 |
| D | PHE143 |
| D | GLY147 |
| D | SER148 |
| D | TYR149 |
| D | GLY150 |
| D | ASN151 |
| D | GLY152 |
| D | MET155 |
| D | HIS182 |
| D | LEU235 |
| D | ILE271 |
| D | ASP314 |
| D | THR317 |
| D | MG402 |
| D | MG403 |
| D | HOH501 |
| D | HOH505 |
| D | HOH513 |
| D | HOH540 |
| D | HOH545 |
| D | HOH567 |
| D | HOH637 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue MG D 402 |
| Chain | Residue |
| D | ASP314 |
| D | ASP316 |
| D | THR317 |
| D | AR6401 |
| D | MG403 |
| D | HOH501 |
| D | HOH513 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue MG D 403 |
| Chain | Residue |
| D | THR76 |
| D | ASP77 |
| D | ASP78 |
| D | ASP316 |
| D | AR6401 |
| D | MG402 |
| D | HOH501 |
| D | HOH534 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | binding site for residue AR6 A 401 |
| Chain | Residue |
| A | THR317 |
| A | MG402 |
| A | MG403 |
| A | HOH501 |
| A | HOH532 |
| A | HOH549 |
| A | HOH579 |
| A | HOH582 |
| A | HOH703 |
| 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 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | THR76 |
| A | ASP77 |
| A | ASP78 |
| A | ASP316 |
| A | AR6401 |
| A | MG403 |
| A | HOH501 |
| A | HOH595 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 403 |
| Chain | Residue |
| A | ASP314 |
| A | ASP316 |
| A | THR317 |
| A | AR6401 |
| A | MG402 |
| A | HOH501 |
| A | HOH532 |
| site_id | AD1 |
| Number of Residues | 24 |
| Details | binding site for residue AR6 B 401 |
| Chain | Residue |
| B | ASP77 |
| B | GLY115 |
| B | GLY117 |
| B | ALA118 |
| B | GLY119 |
| B | VAL120 |
| B | PHE143 |
| B | LYS146 |
| B | GLY147 |
| B | SER148 |
| B | TYR149 |
| B | GLY150 |
| B | ASN151 |
| B | GLY152 |
| B | HIS182 |
| B | ASP314 |
| B | THR317 |
| B | MG402 |
| B | MG403 |
| B | HOH501 |
| B | HOH528 |
| B | HOH554 |
| B | HOH567 |
| B | HOH574 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | ASP314 |
| B | ASP316 |
| B | THR317 |
| B | AR6401 |
| B | MG403 |
| B | HOH501 |
| B | HOH554 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue MG B 403 |
| Chain | Residue |
| B | THR76 |
| B | ASP77 |
| B | ASP78 |
| B | ASP316 |
| B | AR6401 |
| B | MG402 |
| B | HOH501 |
| B | HOH523 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| 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 |
| C | GLU41 | |
| D | GLU41 | |
| A | GLU41 | |
| B | GLU41 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| 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 |
| C | THR76 | |
| D | THR76 | |
| A | THR76 | |
| B | THR76 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| 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 |
| C | ASP77 | |
| B | ASP77 | |
| B | LYS146 | |
| B | HIS182 | |
| C | LYS146 | |
| C | HIS182 | |
| D | ASP77 | |
| D | LYS146 | |
| D | HIS182 | |
| A | ASP77 | |
| A | LYS146 | |
| A | HIS182 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:34321462, ECO:0007744|PDB:7ARW |
| Chain | Residue | Details |
| C | ASP78 | |
| D | ASP78 | |
| A | ASP78 | |
| B | ASP78 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29907568, ECO:0007744|PDB:6D36, ECO:0007744|PDB:6D3A |
| Chain | Residue | Details |
| C | LEU235 | |
| C | ILE271 | |
| D | LEU235 | |
| D | ILE271 | |
| A | LEU235 | |
| A | ILE271 | |
| B | LEU235 | |
| B | ILE271 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| 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 |
| C | ASP314 | |
| C | ASP316 | |
| D | ASP314 | |
| D | ASP316 | |
| A | ASP314 | |
| A | ASP316 | |
| B | ASP314 | |
| B | ASP316 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| 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 |
| C | THR317 | |
| D | THR317 | |
| A | THR317 | |
| B | THR317 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | SITE: Glutamate flap => ECO:0000269|PubMed:29907568, ECO:0000269|PubMed:30045870 |
| Chain | Residue | Details |
| C | GLU41 | |
| D | GLU41 | |
| A | GLU41 | |
| B | GLU41 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| C | THR64 | |
| D | THR64 | |
| A | THR64 | |
| B | THR64 |
