MolNFT v1 · #22621 · protein
Structure of taq DNA polymerase
1TAQ: “Structure of taq DNA polymerase”. X-ray diffraction, 2 ligands (BGL, ZN), 8 pockets (best druggability 0.61). MolNFT v1 #22621 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1TAQ
- Type
- protein
- Length
- 807 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Taq DNA polymerase
- EC
- 2.7.7.7
- UniProt
- P19821
- Ligands
- BGL, ZN
- Pockets
- 8 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Taq DNA polymerase (EC 2.7.7.7) | protein | 807 | 50% helix, 12% strand | P19821 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 219 | 0.61 | 0.82 | 32 | empty |
| 2 | 302 | 0.56 | 0.76 | 30 | empty |
| 3 | 251 | 0.50 | 0.75 | 28 | empty |
| 4 | 172 | 0.49 | 0.77 | 23 | empty |
| 5 | 95 | 0.49 | 0.81 | 20 | empty |
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 P19821
- Elsewhere: RCSB PDB 1TAQ · PDBe 1TAQ · UniProt P19821
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