3L1V
Crystal structure of GmhB from E. coli in complex with calcium 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 |
| 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-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-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 212 |
| Chain | Residue |
| A | CYS112 |
| A | HIS114 |
| A | CYS127 |
| A | CYS129 |
| A | ARG130 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 213 |
| Chain | Residue |
| A | HOH231 |
| A | HOH261 |
| A | HOH350 |
| A | ASP31 |
| A | ASP33 |
| A | ASP156 |
| A | PO4214 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 214 |
| Chain | Residue |
| A | ASP31 |
| A | ARG32 |
| A | ASP33 |
| A | THR73 |
| A | ASN74 |
| A | GLN75 |
| A | LYS131 |
| A | CA213 |
| A | HOH231 |
| A | HOH330 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 212 |
| Chain | Residue |
| B | CYS112 |
| B | HIS114 |
| B | CYS127 |
| B | CYS129 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 213 |
| Chain | Residue |
| B | ASP31 |
| B | ASP33 |
| B | ASP156 |
| B | LYS157 |
| B | PO4214 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 B 214 |
| Chain | Residue |
| B | ASP31 |
| B | ARG32 |
| B | ASP33 |
| B | THR73 |
| B | ASN74 |
| B | LYS131 |
| B | CA213 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"20050699","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"20050614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20050699","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20050614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20050699","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20050614","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Stabilizes the phosphoryl group","evidences":[{"source":"PubMed","id":"20050614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20050699","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Contributes to substrate recognition","evidences":[{"source":"PubMed","id":"20050614","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Site: {"description":"Stabilizes the phosphoryl group","evidences":[{"source":"PubMed","id":"20050614","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lvh |
| Chain | Residue | Details |
| A | ALA100 | |
| A | LYS131 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lvh |
| Chain | Residue | Details |
| B | ALA100 | |
| B | LYS131 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lvh |
| Chain | Residue | Details |
| A | LYS131 | |
| A | THR73 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lvh |
| Chain | Residue | Details |
| B | LYS131 | |
| B | THR73 |
