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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
- 3M7L
- Type
- protein
- Length
- 308 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tellurite resistance protein teha homolog
- UniProt
- P44741
- Pockets
- 8 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tellurite resistance protein teha homolog | protein | 308 | 81% helix, 0% strand | P44741 |
Ligands and binding sites
- BOG · octyl beta-D-glucopyranoside · additive · 5 copies · chains A
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 | 314 | 0.65 | 0.80 | 35 | BOG |
| 2 | 271 | 0.65 | 0.82 | 34 | empty |
| 3 | 128 | 0.61 | 0.85 | 20 | empty |
| 4 | 130 | 0.39 | 0.73 | 22 | empty |
| 5 | 79 | 0.38 | 0.76 | 13 | empty |
Modifications
Observed in the structure: 8 modified (engineered).
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 3M7L · PDBe 3M7L · UniProt P44741
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