1DKL
CRYSTAL STRUCTURE OF ESCHERICHIA COLI PHYTASE AT PH 4.5 (NO LIGAND BOUND)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0003993 | molecular_function | acid phosphatase activity |
| A | 0008252 | molecular_function | nucleotidase activity |
| A | 0008707 | molecular_function | 4-phytase 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 |
| B | 0003924 | molecular_function | GTPase activity |
| B | 0003993 | molecular_function | acid phosphatase activity |
| B | 0008252 | molecular_function | nucleotidase activity |
| B | 0008707 | molecular_function | 4-phytase activity |
| B | 0016036 | biological_process | cellular response to phosphate starvation |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0050308 | molecular_function | sugar-phosphatase activity |
| B | 0052745 | molecular_function | inositol phosphate phosphatase activity |
| B | 0071454 | biological_process | cellular response to anoxia |
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 | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:10655611, ECO:0000305|PubMed:1429631 |
| Chain | Residue | Details |
| A | HIS17 | |
| B | HIS17 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:10655611, ECO:0000305|PubMed:8407904 |
| Chain | Residue | Details |
| A | ASP304 | |
| B | ASP304 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10655611, ECO:0000305|Ref.18, ECO:0007744|PDB:1DKP, ECO:0007744|PDB:1DKQ |
| Chain | Residue | Details |
| A | ARG16 | |
| A | ARG20 | |
| A | ARG92 | |
| A | HIS303 | |
| B | ARG16 | |
| B | ARG20 | |
| B | ARG92 | |
| B | HIS303 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10655611, ECO:0007744|PDB:1DKP, ECO:0007744|PDB:1DKQ |
| Chain | Residue | Details |
| A | ARG267 | |
| B | ARG267 |
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 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1rpt |
| Chain | Residue | Details |
| B | ASP304 | |
| B | HIS17 | |
| B | ARG92 | |
| B | ARG16 | |
| B | ARG20 | |
| B | HIS303 |
