Research workbench
Tas protein from escherichia COLI in complex with NADPH
Analyse Tas protein from escherichia COLI in complex with NADPH in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LQA
- Type
- protein
- Length
- 692 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tas protein
- UniProt
- P0A9T4
- Ligands
- NDP
- Pockets
- 13 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Tas protein | protein | 346 | 42% helix, 15% strand | P0A9T4 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 559 | 0.81 | 0.87 | 73 | NDP |
| 2 | 658 | 0.78 | 0.83 | 83 | NDP |
| 3 | 68 | 0.73 | 0.98 | 20 | empty |
| 4 | 63 | 0.72 | 0.98 | 22 | empty |
| 5 | 83 | 0.55 | 0.86 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1748 Ų buried · 28 hydrogen bonds · protein-protein
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 P0A9T4
- Elsewhere: RCSB PDB 1LQA · PDBe 1LQA · UniProt P0A9T4
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