3Q9L
The structure of the dimeric E.coli MinD-ATP complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000918 | biological_process | division septum site selection |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0007059 | biological_process | chromosome segregation |
| A | 0008298 | biological_process | intracellular mRNA localization |
| A | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0032506 | biological_process | cytokinetic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0051301 | biological_process | cell division |
| A | 0060187 | cellular_component | cell pole |
| B | 0000918 | biological_process | division septum site selection |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0007059 | biological_process | chromosome segregation |
| B | 0008298 | biological_process | intracellular mRNA localization |
| B | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0032506 | biological_process | cytokinetic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0051301 | biological_process | cell division |
| B | 0060187 | cellular_component | cell pole |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 700 |
| Chain | Residue |
| A | THR17 |
| A | HOH261 |
| A | HOH262 |
| A | HOH263 |
| A | ATP800 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ATP A 800 |
| Chain | Residue |
| A | LYS16 |
| A | THR17 |
| A | THR18 |
| A | ALA123 |
| A | ARG182 |
| A | PRO212 |
| A | GLU213 |
| A | ASP214 |
| A | VAL217 |
| A | HOH262 |
| A | HOH263 |
| A | HOH293 |
| A | HOH305 |
| A | HOH310 |
| A | MG700 |
| B | LYS11 |
| B | GLY12 |
| B | GLU146 |
| A | GLY12 |
| A | GLY13 |
| A | VAL14 |
| A | GLY15 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 700 |
| Chain | Residue |
| B | THR17 |
| B | HOH261 |
| B | HOH262 |
| B | HOH263 |
| B | ATP800 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ATP B 800 |
| Chain | Residue |
| A | LYS11 |
| A | GLY12 |
| A | GLU146 |
| B | GLY12 |
| B | GLY13 |
| B | VAL14 |
| B | GLY15 |
| B | LYS16 |
| B | THR17 |
| B | THR18 |
| B | ALA123 |
| B | ARG182 |
| B | ILE211 |
| B | PRO212 |
| B | GLU213 |
| B | ASP214 |
| B | VAL217 |
| B | HOH261 |
| B | HOH263 |
| B | HOH287 |
| B | HOH301 |
| B | HOH312 |
| B | MG700 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q72H90","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
