4YVZ
Structure of Thermotoga maritima DisA in complex with 3'-dATP/Mn2+
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 | 4 |
Details | binding site for residue MN A 401 |
Chain | Residue |
A | ASP75 |
A | 3AT403 |
A | HOH519 |
B | HOH557 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue MN A 402 |
Chain | Residue |
A | GLU229 |
A | ASP232 |
A | ASP233 |
site_id | AC3 |
Number of Residues | 18 |
Details | binding site for residue 3AT A 403 |
Chain | Residue |
A | HOH519 |
A | HOH535 |
B | LEU39 |
B | ASP75 |
B | GLY76 |
B | VAL92 |
B | LEU94 |
B | GLY106 |
B | THR107 |
B | ARG108 |
B | HIS109 |
B | THR111 |
B | SER127 |
B | ARG128 |
B | ARG130 |
B | 3AT401 |
A | ASP75 |
A | MN401 |
site_id | AC4 |
Number of Residues | 19 |
Details | binding site for residue 3AT B 401 |
Chain | Residue |
A | LEU39 |
A | ASP75 |
A | GLY76 |
A | VAL92 |
A | HIS93 |
A | LEU94 |
A | GLY106 |
A | THR107 |
A | ARG108 |
A | HIS109 |
A | THR111 |
A | SER127 |
A | ARG128 |
A | ARG130 |
A | 3AT403 |
B | ASP75 |
B | MN402 |
B | HOH513 |
B | HOH517 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue MN B 402 |
Chain | Residue |
B | ASP75 |
B | 3AT401 |
B | HOH513 |
B | HOH549 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue MN B 403 |
Chain | Residue |
B | GLU229 |
B | ASP232 |
B | ASP233 |
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 |