3VNN
Crystal Structure of a sub-domain of the nucleotidyltransferase (adenylation) domain of human DNA ligase IV
Functional Information from GO Data
Functional Information from PROSITE/UniProt
| site_id | PS00697 |
| Number of Residues | 9 |
| Details | DNA_LIGASE_A1 ATP-dependent DNA ligase AMP-binding site. ETKLDGERM |
| Chain | Residue | Details |
| A | GLU271-MET279 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"N6-AMP-lysine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10135","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23523427","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29980672","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3W1B","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P18858","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23523427","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3W1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3W5O","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23523427","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3W5O","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






