1OID
5'-Nucleotidase (E. coli) with an Engineered Disulfide Bridge (S228C, P513C)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008253 | molecular_function | 5'-nucleotidase activity |
| A | 0008768 | molecular_function | UDP-sugar diphosphatase activity |
| A | 0009166 | biological_process | nucleotide catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008253 | molecular_function | 5'-nucleotidase activity |
| B | 0008768 | molecular_function | UDP-sugar diphosphatase activity |
| B | 0009166 | biological_process | nucleotide catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI A1551 |
| Chain | Residue |
| A | ASP84 |
| A | ASN116 |
| A | HIS217 |
| A | HIS252 |
| A | HOH2114 |
| A | HOH2238 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 34 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1ush |
| Chain | Residue | Details |
| A | ARG375 | |
| A | ARG410 | |
| A | ASP120 | |
| A | HIS117 | |
| A | ARG379 | |
| A | ASN116 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1ush |
| Chain | Residue | Details |
| B | ARG375 | |
| B | ARG410 | |
| B | ASP120 | |
| B | HIS117 | |
| B | ARG379 | |
| B | ASN116 |
| site_id | MCSA1 |
| Number of Residues | 12 |
| Details | M-CSA 611 |
| Chain | Residue | Details |
| A | ASP41 | metal ligand |
| A | ARG375 | electrostatic stabiliser, increase acidity, increase electrophilicity |
| A | ARG379 | electrostatic stabiliser, increase acidity, increase electrophilicity |
| A | ARG410 | electrostatic stabiliser, increase acidity, increase electrophilicity |
| A | HIS43 | metal ligand |
| A | ASP84 | metal ligand |
| A | ASN116 | electrostatic stabiliser, metal ligand |
| A | HIS117 | electrostatic stabiliser, increase nucleophilicity, metal ligand, proton acceptor |
| A | ASP120 | electrostatic stabiliser, increase basicity |
| A | HIS217 | metal ligand |
| A | HIS252 | metal ligand |
| A | GLN254 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 12 |
| Details | M-CSA 611 |
| Chain | Residue | Details |
| B | ASP41 | metal ligand |
| B | ARG375 | electrostatic stabiliser, increase acidity, increase electrophilicity |
| B | ARG379 | electrostatic stabiliser, increase acidity, increase electrophilicity |
| B | ARG410 | electrostatic stabiliser, increase acidity, increase electrophilicity |
| B | HIS43 | metal ligand |
| B | ASP84 | metal ligand |
| B | ASN116 | electrostatic stabiliser, metal ligand |
| B | HIS117 | electrostatic stabiliser, increase nucleophilicity, metal ligand, proton acceptor |
| B | ASP120 | electrostatic stabiliser, increase basicity |
| B | HIS217 | metal ligand |
| B | HIS252 | metal ligand |
| B | GLN254 | metal ligand |
