4YXJ
Structure of Thermotoga maritima DisA in complex with ApCpp
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0004016 | molecular_function | adenylate cyclase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006281 | biological_process | DNA repair |
| A | 0006974 | biological_process | DNA damage response |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0106408 | molecular_function | diadenylate cyclase activity |
| A | 0140097 | molecular_function | catalytic activity, acting on DNA |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0004016 | molecular_function | adenylate cyclase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006281 | biological_process | DNA repair |
| B | 0006974 | biological_process | DNA damage response |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0106408 | molecular_function | diadenylate cyclase activity |
| B | 0140097 | molecular_function | catalytic activity, acting on DNA |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue APC A 401 |
| Chain | Residue |
| A | LEU39 |
| A | SER127 |
| A | ARG128 |
| A | ARG129 |
| A | HOH506 |
| A | HOH513 |
| A | HOH518 |
| B | APC401 |
| A | GLY76 |
| A | VAL92 |
| A | HIS93 |
| A | LEU94 |
| A | GLY106 |
| A | THR107 |
| A | ARG108 |
| A | THR111 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue APC B 401 |
| Chain | Residue |
| A | APC401 |
| A | HOH506 |
| B | LEU39 |
| B | GLY76 |
| B | VAL92 |
| B | HIS93 |
| B | LEU94 |
| B | GLY106 |
| B | THR107 |
| B | ARG108 |
| B | THR111 |
| B | SER127 |
| B | ARG128 |
| B | ARG129 |
| B | ARG130 |
| B | HOH522 |
| B | HOH538 |
| B | HOH541 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 280 |
| Details | Domain: {"description":"DAC","evidences":[{"source":"PROSITE-ProRule","id":"PRU01130","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18439896","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26014055","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3C1Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3C21","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YXM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18439896","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26014055","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3C21","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YXM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18439896","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26014055","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3C21","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
