MolNFT v1 · #4915 · protein
Human thymidylate kinase complexed with ADP, tdp and a magnesium-ion
1E2G: “Human thymidylate kinase complexed with ADP, tdp and a magnesium-ion”. X-ray diffraction, 4 ligands (TMP, ADP, TYD), 1 pocket (best druggability 0.64). MolNFT v1 #4915 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1E2G
- Type
- protein
- Length
- 205 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thymidylate kinase
- EC
- 2.7.4.9
- UniProt
- P23919
- Ligands
- TMP, ADP, TYD, MG
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thymidylate kinase (EC 2.7.4.9) | protein | 205 | 50% helix, 15% strand | P23919 |
Ligands and binding sites
- TMP · Thymidine-5'-phosphate · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- TYD · Thymidine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 174 | 0.64 | 0.85 | 29 | TMP, ADP, TYD, MG |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
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 P23919
- Elsewhere: RCSB PDB 1E2G · PDBe 1E2G · UniProt P23919
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