1DGS
CRYSTAL STRUCTURE OF NAD+-DEPENDENT DNA LIGASE FROM T. FILIFORMIS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003911 | molecular_function | DNA ligase (NAD+) activity |
| A | 0006260 | biological_process | DNA replication |
| A | 0006281 | biological_process | DNA repair |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003911 | molecular_function | DNA ligase (NAD+) activity |
| B | 0006260 | biological_process | DNA replication |
| B | 0006281 | biological_process | DNA repair |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 701 |
| Chain | Residue |
| A | CYS406 |
| A | CYS409 |
| A | CYS422 |
| A | CYS427 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 2701 |
| Chain | Residue |
| B | CYS2406 |
| B | CYS2409 |
| B | CYS2422 |
| B | CYS2427 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AMP A 700 |
| Chain | Residue |
| A | GLU114 |
| A | HIS115 |
| A | LYS116 |
| A | VAL117 |
| A | GLU169 |
| A | ARG196 |
| A | TYR221 |
| A | HIS253 |
| A | LYS312 |
| A | LEU85 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AMP B 2700 |
| Chain | Residue |
| B | HOH1100 |
| B | LEU2085 |
| B | GLU2114 |
| B | HIS2115 |
| B | LYS2116 |
| B | VAL2117 |
| B | LEU2120 |
| B | GLU2169 |
| B | ARG2196 |
| B | TYR2221 |
| B | LYS2312 |
Functional Information from PROSITE/UniProt
| site_id | PS01056 |
| Number of Residues | 16 |
| Details | DNA_LIGASE_N2 NAD-dependent DNA ligase signature 2. VGRTGrVTpVgvLePV |
| Chain | Residue | Details |
| A | VAL329-VAL344 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"N6-AMP-lysine intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01588","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10698952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15268945","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01588","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10698952","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01588","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10698952","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01588","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10698952","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 450 |
| Chain | Residue | Details |
| A | GLU114 | electrostatic stabiliser |
| A | LYS116 | covalent catalysis |
| A | ASP118 | electrostatic stabiliser |
| A | TYR221 | electrostatic stabiliser |
| A | LYS312 | electrostatic stabiliser |
| A | CYS406 | metal ligand |
| A | CYS409 | metal ligand |
| A | CYS422 | metal ligand |
| A | CYS427 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 9 |
| Details | M-CSA 450 |
| Chain | Residue | Details |
| B | GLU2114 | electrostatic stabiliser |
| B | LYS2116 | covalent catalysis |
| B | ASP2118 | electrostatic stabiliser |
| B | TYR2221 | electrostatic stabiliser |
| B | LYS2312 | electrostatic stabiliser |
| B | CYS2406 | metal ligand |
| B | CYS2409 | metal ligand |
| B | CYS2422 | metal ligand |
| B | CYS2427 | metal ligand |
