6U7B
Structure of E. coli MS115-1 CdnC:HORMA-deltaN complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001730 | molecular_function | 2'-5'-oligoadenylate synthetase activity |
A | 0003725 | molecular_function | double-stranded RNA binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005829 | cellular_component | cytosol |
A | 0009117 | biological_process | nucleotide metabolic process |
A | 0016020 | cellular_component | membrane |
A | 0016779 | molecular_function | nucleotidyltransferase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0051607 | biological_process | defense response to virus |
A | 0060700 | biological_process | regulation of ribonuclease activity |
A | 0106408 | molecular_function | diadenylate cyclase activity |
B | 0051607 | biological_process | defense response to virus |
C | 0001730 | molecular_function | 2'-5'-oligoadenylate synthetase activity |
C | 0003725 | molecular_function | double-stranded RNA binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005829 | cellular_component | cytosol |
C | 0009117 | biological_process | nucleotide metabolic process |
C | 0016020 | cellular_component | membrane |
C | 0016779 | molecular_function | nucleotidyltransferase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0051607 | biological_process | defense response to virus |
C | 0060700 | biological_process | regulation of ribonuclease activity |
C | 0106408 | molecular_function | diadenylate cyclase activity |
D | 0051607 | biological_process | defense response to virus |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | binding site for residue MG A 401 |
Chain | Residue |
A | ASP72 |
A | ASP74 |
A | HOH503 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue CL A 402 |
Chain | Residue |
A | GLY59 |
A | SER60 |
A | LEU61 |
A | ASP74 |
A | HOH532 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue ACT B 201 |
Chain | Residue |
B | ASP153 |
B | LYS154 |
B | ACT202 |
B | HOH333 |
B | ASP93 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ACT B 202 |
Chain | Residue |
B | ASP93 |
B | ASN152 |
B | THR155 |
B | ACT201 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ACT B 203 |
Chain | Residue |
B | ARG99 |
B | TYR149 |
B | GLU151 |
D | TYR149 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue MG C 401 |
Chain | Residue |
C | ASP72 |
C | ASP74 |
C | HOH506 |
C | HOH518 |
C | HOH540 |
C | HOH600 |
site_id | AC7 |
Number of Residues | 11 |
Details | binding site for residue AMP C 402 |
Chain | Residue |
C | SER58 |
C | LYS63 |
C | LEU155 |
C | HIS162 |
C | LYS201 |
C | SER202 |
C | PHE203 |
C | ASN270 |
C | VAL272 |
C | HOH522 |
C | HOH552 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue CL C 403 |
Chain | Residue |
C | SER60 |
C | LEU61 |
C | ASP74 |
C | HOH543 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue ACT D 201 |
Chain | Residue |
D | ASP93 |
D | LYS97 |
D | LYS154 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue ACT D 202 |
Chain | Residue |
D | ASP93 |
D | ASN152 |
D | THR155 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:31932165, ECO:0007744|PDB:6P80, ECO:0007744|PDB:6P8V |
Chain | Residue | Details |
A | PRO48 | |
A | ILE147 | |
A | LYS170 | |
A | TYR186 | |
C | PRO48 | |
C | ILE147 | |
C | LYS170 | |
C | TYR186 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:31932165, ECO:0007744|PDB:6U7B |
Chain | Residue | Details |
A | PRO57 | |
C | PRO57 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:31932165, ECO:0007744|PDB:6P80, ECO:0007744|PDB:6P8V, ECO:0007744|PDB:6U7B |
Chain | Residue | Details |
A | GLY59 | |
C | GLY59 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:31932165, ECO:0007744|PDB:6P80 |
Chain | Residue | Details |
A | THR255 | |
C | THR255 |