3L8F
Crystal Structure of D,D-heptose 1.7-bisphosphate phosphatase from E. Coli complexed with magnesium and phosphate
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-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0097171 | biological_process | ADP-L-glycero-beta-D-manno-heptose biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | ASP11 |
| A | ASP13 |
| A | ASP136 |
| A | LYS137 |
| A | HOH291 |
| A | PO4601 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | CYS109 |
| A | ARG110 |
| A | CYS92 |
| A | HIS94 |
| A | CYS107 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 601 |
| Chain | Residue |
| A | ASP11 |
| A | ARG12 |
| A | ASP13 |
| A | THR53 |
| A | ASN54 |
| A | LYS111 |
| A | LYS137 |
| A | HOH207 |
| A | MG401 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:20050699 |
| Chain | Residue | Details |
| A | ASP11 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:20050614, ECO:0000269|PubMed:20050699 |
| Chain | Residue | Details |
| A | ASP13 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20050614 |
| Chain | Residue | Details |
| A | ASP11 | |
| A | LYS137 | |
| A | ASP13 | |
| A | ASP19 | |
| A | CYS92 | |
| A | HIS94 | |
| A | CYS107 | |
| A | CYS109 | |
| A | ARG110 | |
| A | ASP136 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20050614, ECO:0000269|PubMed:20050699 |
| Chain | Residue | Details |
| A | THR53 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | SITE: Stabilizes the phosphoryl group => ECO:0000269|PubMed:20050614, ECO:0000269|PubMed:20050699 |
| Chain | Residue | Details |
| A | THR53 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | SITE: Contributes to substrate recognition => ECO:0000269|PubMed:20050614 |
| Chain | Residue | Details |
| A | ARG110 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | SITE: Stabilizes the phosphoryl group => ECO:0000269|PubMed:20050614 |
| Chain | Residue | Details |
| A | LYS111 |
