Research workbench
Crystal structure of lgg-1 complexed with a weel peptide
Analyse Crystal structure of lgg-1 complexed with a weel peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AZF
- Type
- protein
- Length
- 246 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein lgg-1; Peptide from autophagy-related protein 19
- UniProt
- Q09490, P35193
- Ligands
- CD, SO4
- Pockets
- 1 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein lgg-1 | protein | 119 | 32% helix, 20% strand | Q09490 |
| C, D | Peptide from autophagy-related protein 19 | protein | 4 | 0% helix, 50% strand | P35193 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 389 | 0.72 | 0.83 | 42 | empty |
Interfaces
3 interfaces between chains.
- A–B · 580 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 499 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 483 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 5AZF · Crystal structure of LGG-1 complexed with a WEEL peptide · the same entry in another collection · chain A against A, TM-score 1.00
- P35193 · AlphaFold monomer V2.0 prediction for autophagy-related protein 19 (P35193) · a predicted model of the same protein · chain C against A, TM-score 0.95
- Q09490 · AlphaFold monomer V2.0 prediction for protein lgg-1 (Q09490) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 Q09490
- Every structure of UniProt P35193
- Elsewhere: RCSB PDB 5AZF · PDBe 5AZF · UniProt Q09490 · UniProt P35193
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