3O61
Structure of the E100A E.coli GDP-mannose hydrolase (yffh) in complex with GDP-mannose and Mg++
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006753 | biological_process | nucleoside phosphate metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016818 | molecular_function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides |
| A | 0019693 | biological_process | ribose phosphate metabolic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0052751 | molecular_function | GDP-mannose hydrolase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006753 | biological_process | nucleoside phosphate metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016818 | molecular_function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides |
| B | 0019693 | biological_process | ribose phosphate metabolic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0052751 | molecular_function | GDP-mannose hydrolase activity |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006753 | biological_process | nucleoside phosphate metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016818 | molecular_function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides |
| C | 0019693 | biological_process | ribose phosphate metabolic process |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0052751 | molecular_function | GDP-mannose hydrolase activity |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006753 | biological_process | nucleoside phosphate metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016818 | molecular_function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides |
| D | 0019693 | biological_process | ribose phosphate metabolic process |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0052751 | molecular_function | GDP-mannose hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE GDD A 3846 |
| Chain | Residue |
| A | TYR17 |
| A | ILE129 |
| A | GLU151 |
| A | LYS176 |
| A | MG202 |
| A | HOH206 |
| A | HOH210 |
| B | LYS38 |
| B | ARG39 |
| B | GLU40 |
| B | SER121 |
| A | GLY47 |
| B | PRO122 |
| A | ALA48 |
| A | ARG67 |
| A | ALA85 |
| A | GLY86 |
| A | LEU87 |
| A | GLU104 |
| A | GLU127 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 202 |
| Chain | Residue |
| A | ALA85 |
| A | GLU104 |
| A | HOH206 |
| A | GDD3846 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE NA A 204 |
| Chain | Residue |
| A | THR19 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE GDD B 3846 |
| Chain | Residue |
| A | LYS38 |
| A | ARG39 |
| A | GLU40 |
| A | SER121 |
| A | PRO122 |
| A | GLY123 |
| A | HOH199 |
| B | TYR17 |
| B | PHE18 |
| B | ARG44 |
| B | GLY47 |
| B | ARG67 |
| B | ALA85 |
| B | GLY86 |
| B | LEU87 |
| B | GLU104 |
| B | GLU127 |
| B | ILE129 |
| B | GLU151 |
| B | LYS176 |
| B | HOH196 |
| B | MG202 |
| B | HOH204 |
| B | HOH219 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 202 |
| Chain | Residue |
| B | ALA85 |
| B | GLU104 |
| B | HOH218 |
| B | HOH219 |
| B | GDD3846 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE GDD C 3846 |
| Chain | Residue |
| C | TYR17 |
| C | PHE18 |
| C | ARG44 |
| C | GLY47 |
| C | ALA48 |
| C | ARG67 |
| C | ALA85 |
| C | GLY86 |
| C | LEU87 |
| C | GLU104 |
| C | GLU127 |
| C | ILE129 |
| C | LYS176 |
| C | MG202 |
| C | HOH209 |
| C | HOH215 |
| C | HOH217 |
| C | NA230 |
| D | LYS38 |
| D | ARG39 |
| D | GLU40 |
| D | SER121 |
| D | PRO122 |
| D | GLY123 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 202 |
| Chain | Residue |
| C | ALA85 |
| C | GLU104 |
| C | HOH215 |
| C | HOH217 |
| C | GDD3846 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA C 230 |
| Chain | Residue |
| C | ARG67 |
| C | GLU82 |
| C | SER83 |
| C | ALA85 |
| C | HOH217 |
| C | GDD3846 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE GDD D 3846 |
| Chain | Residue |
| D | LEU87 |
| D | GLU104 |
| D | GLU127 |
| D | ILE129 |
| D | ASP150 |
| D | GLU151 |
| D | LYS176 |
| D | MG202 |
| D | HOH223 |
| C | LYS38 |
| C | ARG39 |
| C | GLU40 |
| C | SER121 |
| C | PRO122 |
| D | TYR17 |
| D | ARG44 |
| D | ARG67 |
| D | ALA85 |
| D | GLY86 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 202 |
| Chain | Residue |
| D | ALA85 |
| D | GLU104 |
| D | HOH223 |
| D | GDD3846 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:21638333, ECO:0007744|PDB:3O61 |
| Chain | Residue | Details |
| A | LYS176 | |
| B | TYR17 | |
| B | ARG67 | |
| B | GLU127 | |
| B | ASP150 | |
| B | LYS176 | |
| C | TYR17 | |
| C | ARG67 | |
| C | GLU127 | |
| C | ASP150 | |
| C | LYS176 | |
| D | TYR17 | |
| D | ARG67 | |
| D | GLU127 | |
| D | ASP150 | |
| D | LYS176 | |
| A | TYR17 | |
| A | ARG67 | |
| A | GLU127 | |
| A | ASP150 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21638333, ECO:0007744|PDB:3O61 |
| Chain | Residue | Details |
| A | LYS38 | |
| B | LYS38 | |
| C | LYS38 | |
| D | LYS38 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21638333, ECO:0007744|PDB:3O6Z |
| Chain | Residue | Details |
| A | GLU104 | |
| A | ALA85 | |
| A | ALA100 | |
| A | GLU151 | |
| B | ALA85 | |
| B | ALA100 | |
| B | GLU104 | |
| B | GLU151 | |
| C | ALA85 | |
| C | ALA100 | |
| C | GLU104 | |
| C | GLU151 | |
| D | ALA85 | |
| D | ALA100 | |
| D | GLU104 | |
| D | GLU151 |
