5D49
Structural Basis for a New Templated Activity by Terminal Deoxynucleotidyl Transferase: Implications for V(D)J Recombination
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 601 |
| Chain | Residue |
| A | ASP343 |
| A | ASP345 |
| A | SO4603 |
| A | HOH720 |
| A | HOH852 |
| C | DC8 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 602 |
| Chain | Residue |
| A | HOH1003 |
| C | DG6 |
| C | HOH104 |
| A | THR253 |
| A | VAL255 |
| A | VAL258 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue SO4 A 603 |
| Chain | Residue |
| A | GLY332 |
| A | GLY333 |
| A | ARG336 |
| A | ASP345 |
| A | MG601 |
| A | HOH756 |
| A | HOH777 |
| A | HOH852 |
| A | HOH944 |
| C | DC8 |
| C | HOH107 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 604 |
| Chain | Residue |
| A | GLY425 |
| A | LYS426 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 605 |
| Chain | Residue |
| A | ASN184 |
| A | GLY186 |
| A | SER187 |
| A | HOH848 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 606 |
| Chain | Residue |
| A | LYS338 |
| A | MET339 |
| A | THR340 |
| A | HOH796 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue ACT A 607 |
| Chain | Residue |
| A | GLY213 |
| A | LYS222 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue PG4 A 608 |
| Chain | Residue |
| A | PRO324 |
| A | ASP325 |
| A | GLU352 |
| A | HOH770 |
Functional Information from PROSITE/UniProt
| site_id | PS00522 |
| Number of Residues | 20 |
| Details | DNA_POLYMERASE_X DNA polymerase family X signature. GGFrRGkmtGhDVDFLItsP |
| Chain | Residue | Details |
| A | GLY332-PRO351 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Region: {"description":"Involved in DNA binding","evidences":[{"source":"PubMed","id":"11823435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23856622","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4I2B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I2C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I2D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I2E","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 632 |
| Chain | Residue | Details |
| A | ASP343 | metal ligand |
| A | ASP345 | metal ligand |
| A | ASP434 | metal ligand, proton acceptor, proton donor |
