6P8V
Structure of E. coli MS115-1 HORMA:CdnC:Trip13 complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0015630 | cellular_component | microtubule cytoskeleton |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0051607 | biological_process | defense response to virus |
| B | 0005524 | molecular_function | ATP binding |
| B | 0015630 | cellular_component | microtubule cytoskeleton |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0051607 | biological_process | defense response to virus |
| C | 0005524 | molecular_function | ATP binding |
| C | 0015630 | cellular_component | microtubule cytoskeleton |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0051607 | biological_process | defense response to virus |
| D | 0005524 | molecular_function | ATP binding |
| D | 0015630 | cellular_component | microtubule cytoskeleton |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0051607 | biological_process | defense response to virus |
| E | 0005524 | molecular_function | ATP binding |
| E | 0015630 | cellular_component | microtubule cytoskeleton |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0051607 | biological_process | defense response to virus |
| F | 0005524 | molecular_function | ATP binding |
| F | 0015630 | cellular_component | microtubule cytoskeleton |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0051607 | biological_process | defense response to virus |
| G | 0001730 | molecular_function | 2'-5'-oligoadenylate synthetase activity |
| G | 0003725 | molecular_function | double-stranded RNA binding |
| G | 0005524 | molecular_function | ATP binding |
| G | 0005829 | cellular_component | cytosol |
| G | 0009117 | biological_process | nucleotide metabolic process |
| G | 0016020 | cellular_component | membrane |
| G | 0016779 | molecular_function | nucleotidyltransferase activity |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0051607 | biological_process | defense response to virus |
| G | 0060700 | biological_process | regulation of ribonuclease activity |
| G | 0106408 | molecular_function | diadenylate cyclase activity |
| H | 0051607 | biological_process | defense response to virus |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue ATP B 401 |
| Chain | Residue |
| A | LEU29 |
| A | ASN204 |
| A | PHE268 |
| A | THR272 |
| A | GLN273 |
| B | ARG215 |
| B | ARG216 |
| A | VAL30 |
| A | LEU32 |
| A | GLY84 |
| A | SER85 |
| A | GLY86 |
| A | LYS87 |
| A | THR88 |
| A | GLU89 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue ATP B 402 |
| Chain | Residue |
| B | LEU29 |
| B | VAL30 |
| B | LEU32 |
| B | GLY84 |
| B | SER85 |
| B | GLY86 |
| B | LYS87 |
| B | THR88 |
| B | GLU89 |
| B | ASN204 |
| B | PHE268 |
| B | SER269 |
| B | THR272 |
| B | GLN273 |
| C | ARG215 |
| C | ARG216 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue ATP C 401 |
| Chain | Residue |
| C | VAL30 |
| C | VAL83 |
| C | GLY84 |
| C | SER85 |
| C | GLY86 |
| C | LYS87 |
| C | THR88 |
| C | GLU89 |
| C | ASP158 |
| C | PHE268 |
| C | SER269 |
| C | THR272 |
| C | GLN273 |
| D | ASP188 |
| D | ARG215 |
| D | ARG216 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | binding site for residue ATP D 401 |
| Chain | Residue |
| D | ARG28 |
| D | LEU29 |
| D | VAL30 |
| D | LEU32 |
| D | ASP82 |
| D | VAL83 |
| D | GLY84 |
| D | SER85 |
| D | GLY86 |
| D | LYS87 |
| D | THR88 |
| D | GLU89 |
| D | LEU234 |
| D | PHE268 |
| D | SER269 |
| D | THR272 |
| D | GLN273 |
| E | ARG72 |
| E | ASP188 |
| E | ARG215 |
| E | ARG216 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | binding site for residue ATP G 401 |
| Chain | Residue |
| G | SER58 |
| G | GLY59 |
| G | SER60 |
| G | LYS63 |
| G | LEU70 |
| G | ASP74 |
| G | LEU155 |
| G | HIS162 |
| G | LYS185 |
| G | LYS201 |
| G | SER202 |
| G | PHE203 |
| G | ASP264 |
| G | ASN270 |
| G | MG402 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue MG G 402 |
| Chain | Residue |
| G | ASP74 |
| G | ATP401 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31932165, ECO:0007744|PDB:6P80, ECO:0007744|PDB:6P8V |
| Chain | Residue | Details |
| G | PRO48 | |
| E | ARG215 | |
| F | GLY84 | |
| F | ARG215 | |
| G | ILE147 | |
| G | LYS170 | |
| G | TYR186 | |
| C | GLY84 | |
| C | ARG215 | |
| D | GLY84 | |
| D | ARG215 | |
| E | GLY84 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31932165, ECO:0007744|PDB:6U7B |
| Chain | Residue | Details |
| G | PRO57 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31932165, ECO:0007744|PDB:6P80, ECO:0007744|PDB:6P8V, ECO:0007744|PDB:6U7B |
| Chain | Residue | Details |
| G | GLY59 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31932165, ECO:0007744|PDB:6P80 |
| Chain | Residue | Details |
| G | THR255 |
