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 | 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 |
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 |