4L57
High resolutin structure of human cytosolic 5'(3')-deoxyribonucleotidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000255 | biological_process | allantoin metabolic process |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0006204 | biological_process | IMP catabolic process |
| A | 0006249 | biological_process | dCMP catabolic process |
| A | 0008252 | molecular_function | nucleotidase activity |
| A | 0008253 | molecular_function | 5'-nucleotidase activity |
| A | 0009117 | biological_process | nucleotide metabolic process |
| A | 0009223 | biological_process | pyrimidine deoxyribonucleotide catabolic process |
| A | 0009264 | biological_process | deoxyribonucleotide catabolic process |
| A | 0016311 | biological_process | dephosphorylation |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0019103 | molecular_function | pyrimidine nucleotide binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043605 | biological_process | amide catabolic process |
| A | 0046050 | biological_process | UMP catabolic process |
| A | 0046055 | biological_process | dGMP catabolic process |
| A | 0046074 | biological_process | dTMP catabolic process |
| A | 0046079 | biological_process | dUMP catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000255 | biological_process | allantoin metabolic process |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| B | 0006204 | biological_process | IMP catabolic process |
| B | 0006249 | biological_process | dCMP catabolic process |
| B | 0008252 | molecular_function | nucleotidase activity |
| B | 0008253 | molecular_function | 5'-nucleotidase activity |
| B | 0009117 | biological_process | nucleotide metabolic process |
| B | 0009223 | biological_process | pyrimidine deoxyribonucleotide catabolic process |
| B | 0009264 | biological_process | deoxyribonucleotide catabolic process |
| B | 0016311 | biological_process | dephosphorylation |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016791 | molecular_function | phosphatase activity |
| B | 0019103 | molecular_function | pyrimidine nucleotide binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043605 | biological_process | amide catabolic process |
| B | 0046050 | biological_process | UMP catabolic process |
| B | 0046055 | biological_process | dGMP catabolic process |
| B | 0046074 | biological_process | dTMP catabolic process |
| B | 0046079 | biological_process | dUMP catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 201 |
| Chain | Residue |
| A | ASP10 |
| A | ASP12 |
| A | ASP145 |
| A | PO4202 |
| A | HOH311 |
| A | HOH320 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PO4 A 202 |
| Chain | Residue |
| A | THR99 |
| A | SER100 |
| A | LYS112 |
| A | LYS134 |
| A | MG201 |
| A | GOL204 |
| A | HOH301 |
| A | HOH311 |
| A | HOH320 |
| A | HOH535 |
| A | ASP10 |
| A | MET11 |
| A | ASP12 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 203 |
| Chain | Residue |
| A | ASN186 |
| A | ARG188 |
| A | GLU189 |
| A | HOH335 |
| A | HOH391 |
| A | HOH524 |
| B | HOH336 |
| B | HOH353 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 204 |
| Chain | Residue |
| A | PHE18 |
| A | GLU19 |
| A | PHE44 |
| A | PO4202 |
| A | GOL207 |
| A | HOH320 |
| A | HOH326 |
| A | HOH500 |
| A | HOH510 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 205 |
| Chain | Residue |
| A | PHE44 |
| A | SER100 |
| A | ARG132 |
| A | HOH301 |
| A | HOH389 |
| A | HOH546 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 206 |
| Chain | Residue |
| A | ARG51 |
| A | ASP59 |
| A | GLU117 |
| A | GLN118 |
| A | HOH318 |
| A | HOH332 |
| A | HOH520 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 207 |
| Chain | Residue |
| A | PHE18 |
| A | PHE44 |
| A | LEU45 |
| A | ALA46 |
| A | ARG47 |
| A | TYR65 |
| A | GOL204 |
| A | HOH410 |
| A | HOH511 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 208 |
| Chain | Residue |
| A | ASN88 |
| A | LEU90 |
| A | THR93 |
| A | HOH423 |
| A | HOH429 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 201 |
| Chain | Residue |
| B | ASP10 |
| B | ASP12 |
| B | ASP145 |
| B | PO4202 |
| B | HOH314 |
| B | HOH315 |
| site_id | BC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PO4 B 202 |
| Chain | Residue |
| B | ASP10 |
| B | MET11 |
| B | ASP12 |
| B | THR99 |
| B | SER100 |
| B | LYS112 |
| B | LYS134 |
| B | MG201 |
| B | GOL203 |
| B | HOH301 |
| B | HOH314 |
| B | HOH315 |
| B | HOH371 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 203 |
| Chain | Residue |
| B | ASP12 |
| B | PHE18 |
| B | PHE44 |
| B | LEU45 |
| B | PHE71 |
| B | LEU102 |
| B | PO4202 |
| B | HOH371 |
| B | HOH384 |
| B | HOH479 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
