1T8Q
Structural genomics, Crystal structure of Glycerophosphoryl diester phosphodiesterase from E. coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008081 | molecular_function | phosphoric diester hydrolase activity |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008081 | molecular_function | phosphoric diester hydrolase activity |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0008081 | molecular_function | phosphoric diester hydrolase activity |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0008081 | molecular_function | phosphoric diester hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1601 |
| Chain | Residue |
| A | GLU63 |
| A | ASP65 |
| A | GLU171 |
| A | GOL1605 |
| A | HOH1615 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1602 |
| Chain | Residue |
| B | HOH1612 |
| B | GLU63 |
| B | ASP65 |
| B | GLU171 |
| B | GOL1606 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 1603 |
| Chain | Residue |
| C | GLU63 |
| C | ASP65 |
| C | GLU171 |
| C | GOL1607 |
| C | HOH1614 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 1604 |
| Chain | Residue |
| D | GLU63 |
| D | ASP65 |
| D | GLU171 |
| D | GOL1608 |
| D | HOH1616 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GOL A 1605 |
| Chain | Residue |
| A | HIS36 |
| A | ARG37 |
| A | GLU63 |
| A | ASP65 |
| A | GLU171 |
| A | LYS173 |
| A | TYR313 |
| A | MG1601 |
| A | HOH1615 |
| A | HOH1616 |
| A | HOH1657 |
| A | HOH1905 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL B 1606 |
| Chain | Residue |
| B | HIS36 |
| B | ARG37 |
| B | GLU63 |
| B | ASP65 |
| B | GLU171 |
| B | LYS173 |
| B | PHE210 |
| B | MG1602 |
| B | HOH1612 |
| B | HOH1613 |
| B | HOH1677 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL C 1607 |
| Chain | Residue |
| C | HIS36 |
| C | ARG37 |
| C | GLU63 |
| C | GLU171 |
| C | LYS173 |
| C | PHE210 |
| C | TYR313 |
| C | MG1603 |
| C | HOH1653 |
| C | HOH1739 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL D 1608 |
| Chain | Residue |
| D | HIS36 |
| D | ARG37 |
| D | GLU63 |
| D | ASP65 |
| D | GLU171 |
| D | LYS173 |
| D | PHE210 |
| D | MG1604 |
| D | HOH1616 |
| D | HOH1639 |
| D | HOH1746 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1609 |
| Chain | Residue |
| A | LYS195 |
| A | HOH1811 |
| A | HOH1955 |
| A | HOH1962 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 1610 |
| Chain | Residue |
| B | LYS195 |
| B | HOH1847 |
| B | HOH1870 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 1611 |
| Chain | Residue |
| B | LYS140 |
| C | LYS195 |
| C | TYR196 |
| C | HOH1750 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL D 1612 |
| Chain | Residue |
| D | LYS195 |
| D | TYR196 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 1613 |
| Chain | Residue |
| C | ARG95 |
| C | ALA96 |
| C | ASP106 |
| C | HOH1862 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1614 |
| Chain | Residue |
| A | ARG95 |
| A | ASP106 |
| A | HOH1779 |
| A | HOH1909 |
| A | HOH1910 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 1615 |
| Chain | Residue |
| D | ARG95 |
| D | ARG97 |
| D | ASP106 |
| D | HOH1728 |
| D | HOH1736 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q8RB32","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q8RB32","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2005","submissionDatabase":"PDB data bank","title":"Crystal structure of periplasmic glycerophosphodiester phosphodiesterase from Escherichia coli.","authoringGroup":["New York structural genomix research consortium (NYSGXRC)"]}},{"source":"PDB","id":"1T8Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YDY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
