1TE2
Putative Phosphatase Ynic from Escherichia coli K12
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003850 | molecular_function | 2-deoxyglucose-6-phosphatase activity |
| A | 0004346 | molecular_function | glucose-6-phosphatase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050084 | molecular_function | mannitol-1-phosphatase activity |
| A | 0050286 | molecular_function | sorbitol-6-phosphatase activity |
| A | 0050308 | molecular_function | sugar-phosphatase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003850 | molecular_function | 2-deoxyglucose-6-phosphatase activity |
| B | 0004346 | molecular_function | glucose-6-phosphatase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016791 | molecular_function | phosphatase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050084 | molecular_function | mannitol-1-phosphatase activity |
| B | 0050286 | molecular_function | sorbitol-6-phosphatase activity |
| B | 0050308 | molecular_function | sugar-phosphatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PGA A 711 |
| Chain | Residue |
| A | ASP13 |
| A | HOH720 |
| A | MSE14 |
| A | ASP15 |
| A | GLY51 |
| A | SER115 |
| A | ALA116 |
| A | LYS148 |
| A | CA702 |
| A | HOH713 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PGA B 712 |
| Chain | Residue |
| B | ASP13 |
| B | MSE14 |
| B | ASP15 |
| B | GLY51 |
| B | SER115 |
| B | ALA116 |
| B | LYS148 |
| B | CA704 |
| B | HOH716 |
| B | HOH860 |
| B | HOH924 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 701 |
| Chain | Residue |
| A | ASP130 |
| A | ASP133 |
| A | HOH738 |
| B | ASP130 |
| B | ASP133 |
| B | HOH743 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 702 |
| Chain | Residue |
| A | ASP13 |
| A | ASP15 |
| A | ASP173 |
| A | PGA711 |
| A | HOH713 |
| A | HOH720 |
| A | HOH725 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA B 703 |
| Chain | Residue |
| B | GLU106 |
| B | HOH829 |
| B | HOH927 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 704 |
| Chain | Residue |
| B | ASP13 |
| B | ASP15 |
| B | ASP173 |
| B | PGA712 |
| B | HOH716 |
| B | HOH740 |
| B | HOH924 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"Q8CHP8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q8CHP8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2004","submissionDatabase":"PDB data bank","title":"Crystal structure of putative phosphatase YniC from Escherichia coli K12.","authors":["Kim Y.","Joachimiak A.","Evdokimova E.","Savchenko A.","Edwards A.M."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"AUG-2004","submissionDatabase":"PDB data bank","title":"Crystal structure of putative phosphatase YniC from Escherichia coli K12.","authors":["Kim Y.","Joachimiak A.","Evdokimova E.","Savchenko A.","Edwards A.M."]}}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lvh |
| Chain | Residue | Details |
| A | SER117 | |
| A | LYS148 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lvh |
| Chain | Residue | Details |
| B | SER117 | |
| B | LYS148 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lvh |
| Chain | Residue | Details |
| A | LYS148 | |
| A | SER115 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lvh |
| Chain | Residue | Details |
| B | LYS148 | |
| B | SER115 |
