1TE2
Putative Phosphatase Ynic from Escherichia coli K12
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003850 | molecular_function | 2-deoxyglucose-6-phosphatase activity |
A | 0004346 | molecular_function | glucose-6-phosphatase activity |
A | 0005829 | cellular_component | cytosol |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016791 | molecular_function | phosphatase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0050084 | molecular_function | mannitol-1-phosphatase activity |
A | 0050286 | molecular_function | sorbitol-6-phosphatase activity |
A | 0050308 | molecular_function | sugar-phosphatase activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003850 | molecular_function | 2-deoxyglucose-6-phosphatase activity |
B | 0004346 | molecular_function | glucose-6-phosphatase activity |
B | 0005829 | cellular_component | cytosol |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016791 | molecular_function | phosphatase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0050084 | molecular_function | mannitol-1-phosphatase activity |
B | 0050286 | molecular_function | sorbitol-6-phosphatase activity |
B | 0050308 | molecular_function | sugar-phosphatase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PGA A 711 |
Chain | Residue |
A | ASP13 |
A | HOH720 |
A | MSE14 |
A | ASP15 |
A | GLY51 |
A | SER115 |
A | ALA116 |
A | LYS148 |
A | CA702 |
A | HOH713 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PGA B 712 |
Chain | Residue |
B | ASP13 |
B | MSE14 |
B | ASP15 |
B | GLY51 |
B | SER115 |
B | ALA116 |
B | LYS148 |
B | CA704 |
B | HOH716 |
B | HOH860 |
B | HOH924 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 701 |
Chain | Residue |
A | ASP130 |
A | ASP133 |
A | HOH738 |
B | ASP130 |
B | ASP133 |
B | HOH743 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 702 |
Chain | Residue |
A | ASP13 |
A | ASP15 |
A | ASP173 |
A | PGA711 |
A | HOH713 |
A | HOH720 |
A | HOH725 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA B 703 |
Chain | Residue |
B | GLU106 |
B | HOH829 |
B | HOH927 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA B 704 |
Chain | Residue |
B | ASP13 |
B | ASP15 |
B | ASP173 |
B | PGA712 |
B | HOH716 |
B | HOH740 |
B | HOH924 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q8CHP8 |
Chain | Residue | Details |
A | ASP13 | |
B | ASP13 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q8CHP8 |
Chain | Residue | Details |
A | ASP15 | |
B | ASP15 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|Ref.7 |
Chain | Residue | Details |
A | ASP13 | |
A | ASP15 | |
A | ASP173 | |
B | ASP13 | |
B | ASP15 | |
B | ASP173 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|Ref.7 |
Chain | Residue | Details |
A | SER115 | |
A | LYS148 | |
B | SER115 | |
B | LYS148 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1lvh |
Chain | Residue | Details |
A | SER117 | |
A | LYS148 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1lvh |
Chain | Residue | Details |
B | SER117 | |
B | LYS148 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1lvh |
Chain | Residue | Details |
A | LYS148 | |
A | SER115 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1lvh |
Chain | Residue | Details |
B | LYS148 | |
B | SER115 |