Research workbench
Crystal structure of the catalytic core of murine terminal deoxynucleotidyl transferase
Analyse Crystal structure of the catalytic core of murine terminal deoxynucleotidyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JMS
- Type
- protein
- Length
- 360 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Terminal deoxynucleotidyltransferase
- EC
- 2.7.7.31
- UniProt
- P09838
- Ligands
- MG, NA
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Terminal deoxynucleotidyltransferase (EC 2.7.7.31) | protein | 360 | 49% helix, 14% strand | P09838 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 810 | 0.68 | 0.75 | 68 | MG, NA |
| 2 | 72 | 0.38 | 0.78 | 16 | empty |
Compared structures
- 1JMS · Crystal Structure of the Catalytic Core of Murine Terminal Deoxynucleotidyl Transferase · the same entry in another collection · chain A against A, TM-score 1.00
- P09838 · AlphaFold monomer V2.0 prediction for DNA nucleotidylexotransferase (P09838) · a predicted model of the same protein · chain A against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P09838
- Elsewhere: RCSB PDB 1JMS · PDBe 1JMS · UniProt P09838
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