1NT4
Crystal structure of Escherichia coli periplasmic glucose-1-phosphatase H18A mutant complexed with glucose-1-phosphate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006007 | biological_process | glucose catabolic process |
A | 0008877 | molecular_function | glucose-1-phosphatase activity |
A | 0016158 | molecular_function | 3-phytase activity |
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 |
B | 0006007 | biological_process | glucose catabolic process |
B | 0008877 | molecular_function | glucose-1-phosphatase activity |
B | 0016158 | molecular_function | 3-phytase activity |
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 |
Functional Information from PROSITE/UniProt
site_id | PS00778 |
Number of Residues | 17 |
Details | HIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. ItVLvGHDSNIasLltA |
Chain | Residue | Details |
A | ILE283-ALA299 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
A | ALA18 | |
B | ALA1018 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | ASP290 | |
B | ASP1290 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: |
Chain | Residue | Details |
A | ARG17 | |
B | HIS1289 | |
A | ARG21 | |
A | ARG94 | |
A | GLU196 | |
A | HIS289 | |
B | ARG1017 | |
B | ARG1021 | |
B | ARG1094 | |
B | GLU1196 |