Research workbench
Crystal Structure of Plant SLAC1 homolog TehA
Analyse Crystal Structure of Plant SLAC1 homolog TehA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3M73
- Type
- protein
- Length
- 313 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.15
- Source
- Haemophilus influenzae
- Molecule
- Tellurite resistance protein tehA homolog
- UniProt
- P44741
- Pockets
- 7 · best druggability 0.69
Structure
x-ray diffraction · resolution 1.15 · 1 distinct chain · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tellurite resistance protein tehA homolog | protein | 313 | 80% helix, 0% strand | P44741 |
Ligands and binding sites
- BOG · octyl beta-D-glucopyranoside · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 262 | 0.69 | 0.84 | 37 | empty |
| 2 | 325 | 0.65 | 0.80 | 37 | empty |
| 3 | 116 | 0.55 | 0.82 | 15 | empty |
| 4 | 75 | 0.37 | 0.76 | 11 | empty |
| 5 | 107 | 0.36 | 0.73 | 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 P44741
- Elsewhere: RCSB PDB 3M73 · PDBe 3M73 · UniProt P44741
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.