1DKO
CRYSTAL STRUCTURE OF TUNGSTATE COMPLEX OF ESCHERICHIA COLI PHYTASE AT PH 6.6 WITH TUNGSTATE BOUND AT THE ACTIVE SITE AND WITH HG2+ CATION ACTING AS AN INTERMOLECULAR BRIDGE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0008252 | molecular_function | nucleotidase activity |
| A | 0016036 | biological_process | cellular response to phosphate starvation |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0050308 | molecular_function | sugar-phosphatase activity |
| A | 0052745 | molecular_function | inositol phosphate phosphatase activity |
| A | 0071454 | biological_process | cellular response to anoxia |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG A 500 |
| Chain | Residue |
| A | HIS113 |
| A | ASP154 |
| A | HIS158 |
| A | TYR289 |
| A | HOH612 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE HG A 501 |
| Chain | Residue |
| A | ASP325 |
| A | THR327 |
| A | ARG16 |
| A | GLU219 |
| A | HIS250 |
| A | ASP304 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG A 502 |
| Chain | Residue |
| A | GLN285 |
| A | LYS286 |
| A | LEU293 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG A 503 |
| Chain | Residue |
| A | ALA278 |
| A | PRO294 |
| A | THR295 |
| A | HOH843 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE WO4 A 504 |
| Chain | Residue |
| A | ARG16 |
| A | HIS17 |
| A | ARG20 |
| A | ARG92 |
| A | HIS303 |
| A | ASP304 |
| A | HOH660 |
Functional Information from PROSITE/UniProt
| site_id | PS00616 |
| Number of Residues | 15 |
| Details | HIS_ACID_PHOSPHAT_1 Histidine acid phosphatases phosphohistidine signature. LesVviVsRHGvRaP |
| Chain | Residue | Details |
| A | LEU8-PRO22 |
| site_id | PS00778 |
| Number of Residues | 17 |
| Details | HIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. VlFIaGHDTNLanLggA |
| Chain | Residue | Details |
| A | VAL297-ALA313 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10655611","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"1429631","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"10655611","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8407904","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10655611","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"JUN-2014","submissionDatabase":"PDB data bank","title":"The Complex Structure of mutant Phytase with IHS.","authors":["Wu T.H.","Chen C.C.","Huang C.H.","Guo R.T."]}},{"source":"PDB","id":"1DKP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DKQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10655611","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DKP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DKQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rpt |
| Chain | Residue | Details |
| A | ASP304 | |
| A | HIS17 | |
| A | ARG92 | |
| A | ARG16 | |
| A | ARG20 | |
| A | HIS303 |
