2GMW
Crystal Structure of D,D-heptose 1.7-bisphosphate phosphatase from E. Coli.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| A | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0034200 | molecular_function | D,D-heptose 1,7-bisphosphate phosphatase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0097171 | biological_process | ADP-L-glycero-beta-D-manno-heptose biosynthetic process |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| B | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016791 | molecular_function | phosphatase activity |
| B | 0034200 | molecular_function | D,D-heptose 1,7-bisphosphate phosphatase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0097171 | biological_process | ADP-L-glycero-beta-D-manno-heptose biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 300 |
| Chain | Residue |
| A | CYS112 |
| A | HIS114 |
| A | CYS127 |
| A | CYS129 |
| A | ARG130 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 300 |
| Chain | Residue |
| B | ARG130 |
| B | CYS112 |
| B | HIS114 |
| B | CYS127 |
| B | CYS129 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:20050699 |
| Chain | Residue | Details |
| A | ASP31 | |
| B | ASP31 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:20050614, ECO:0000269|PubMed:20050699 |
| Chain | Residue | Details |
| A | ASP33 | |
| B | ASP33 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20050614 |
| Chain | Residue | Details |
| A | ASP31 | |
| A | LYS157 | |
| B | ASP31 | |
| B | ASP33 | |
| B | ASP39 | |
| B | CYS112 | |
| B | HIS114 | |
| B | CYS127 | |
| B | CYS129 | |
| B | ARG130 | |
| B | ASP156 | |
| A | ASP33 | |
| B | LYS157 | |
| A | ASP39 | |
| A | CYS112 | |
| A | HIS114 | |
| A | CYS127 | |
| A | CYS129 | |
| A | ARG130 | |
| A | ASP156 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20050614, ECO:0000269|PubMed:20050699 |
| Chain | Residue | Details |
| A | THR73 | |
| B | THR73 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Stabilizes the phosphoryl group => ECO:0000269|PubMed:20050614, ECO:0000269|PubMed:20050699 |
| Chain | Residue | Details |
| A | THR73 | |
| B | THR73 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Contributes to substrate recognition => ECO:0000269|PubMed:20050614 |
| Chain | Residue | Details |
| A | ARG130 | |
| B | ARG130 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | SITE: Stabilizes the phosphoryl group => ECO:0000269|PubMed:20050614 |
| Chain | Residue | Details |
| A | LYS131 | |
| B | LYS131 |
