6RMR
Crystal structure of Escherichia coli periplasmic glucose-1-phosphatase H18D mutant
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 | inositol hexakisphosphate 3-phosphatase 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 | inositol hexakisphosphate 3-phosphatase 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 PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue 1PE A 401 |
| Chain | Residue |
| A | GLU196 |
| A | HIS289 |
| A | ASP290 |
| A | SER291 |
| A | ACT407 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 402 |
| Chain | Residue |
| A | THR104 |
| A | CYS110 |
| A | ILE112 |
| B | ACT402 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue ACT A 403 |
| Chain | Residue |
| A | CYS79 |
| A | PRO80 |
| A | ASP111 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue ACT A 404 |
| Chain | Residue |
| A | GLN93 |
| A | GLY121 |
| A | HOH518 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue ACT A 405 |
| Chain | Residue |
| A | LEU297 |
| A | THR298 |
| A | PHE302 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue ACT A 406 |
| Chain | Residue |
| A | LEU182 |
| A | HOH503 |
| B | GLU5 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue ACT A 407 |
| Chain | Residue |
| A | ARG17 |
| A | ASP18 |
| A | ARG94 |
| A | HIS289 |
| A | ASP290 |
| A | 1PE401 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue ACT A 408 |
| Chain | Residue |
| A | LEU9 |
| A | GLN10 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue ZN A 409 |
| Chain | Residue |
| A | ASP270 |
| A | ASP383 |
| A | ASN387 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue ACT B 401 |
| Chain | Residue |
| B | TRP237 |
| B | ASN311 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue ACT B 402 |
| Chain | Residue |
| A | ACT402 |
| B | THR104 |
| B | ILE112 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue ACT B 403 |
| Chain | Residue |
| A | HIS326 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue ACT B 404 |
| Chain | Residue |
| B | ASN167 |
| B | LYS169 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue ACT B 405 |
| Chain | Residue |
| A | GLN306 |
| A | VAL362 |
| B | ASP380 |
| B | ASP383 |
| B | ASN387 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue ACT B 406 |
| Chain | Residue |
| B | ASP18 |
| B | ARG94 |
| B | HIS289 |
| B | ASP290 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue ACT B 407 |
| Chain | Residue |
| B | TYR88 |
| B | GLN117 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue ACT B 408 |
| Chain | Residue |
| B | GLN48 |
| B | LEU92 |
| B | GLN93 |
| B | GLY121 |
| B | HOH518 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue ACT B 409 |
| Chain | Residue |
| A | SER76 |
| A | PRO108 |
| B | VAL44 |
| B | GLN48 |
| site_id | AE1 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 410 |
| Chain | Residue |
| B | GLU196 |
| B | SER291 |
| site_id | AE2 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 411 |
| Chain | Residue |
| B | GLU219 |
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 | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {} |
| Chain | Residue | Details |
