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Crystal structure of human LC3A_2-121
Analyse Crystal structure of human LC3A_2-121 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WAL
- Type
- protein
- Length
- 115 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Homo sapiens
- Molecule
- Microtubule-associated proteins 1A/1B light chain 3A
- UniProt
- Q9H492
- Ligands
- MLT
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 33% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Microtubule-associated proteins 1A/1B light chain 3A | protein | 115 | 33% helix, 23% strand | Q9H492 |
Ligands and binding sites
- MLT · D-malate · ligand · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 57 | 0.29 | 0.74 | 16 | 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 Q9H492
- Elsewhere: RCSB PDB 3WAL · PDBe 3WAL · UniProt Q9H492
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