1SPV
Crystal Structure of the Putative Phosphatase of Escherichia coli, Northeast Structural Genomoics Target ER58
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001883 | molecular_function | purine nucleoside binding |
| A | 0008428 | molecular_function | ribonuclease inhibitor activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019213 | molecular_function | deacetylase activity |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0042278 | biological_process | purine nucleoside metabolic process |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0060698 | molecular_function | endoribonuclease inhibitor activity |
| A | 0061463 | molecular_function | O-acetyl-ADP-ribose deacetylase activity |
| A | 1900231 | biological_process | regulation of single-species biofilm formation on inanimate substrate |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MES A 201 |
| Chain | Residue |
| A | ALA23 |
| A | HOH275 |
| A | ASN25 |
| A | GLY32 |
| A | ASP35 |
| A | ASP48 |
| A | SER122 |
| A | GLY124 |
| A | VAL125 |
| A | TYR126 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01205","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26481419","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01205","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26481419","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
