Research workbench
Human GID4 bound to a GLY/N-peptide
Analyse Human GID4 bound to a GLY/N-peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Q4Y
- Type
- protein
- Length
- 342 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucose-induced degradation protein 4 homolog
- UniProt
- Q8IVV7
- Pockets
- 8 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucose-induced degradation protein 4 homolog | protein | 168 | 5% helix, 42% strand | Q8IVV7 |
| B | Glucose-induced degradation protein 4 homolog | protein | 174 | 9% helix, 39% strand | Q8IVV7 |
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 | 187 | 0.60 | 0.82 | 27 | empty |
| 2 | 155 | 0.58 | 0.82 | 27 | empty |
| 3 | 194 | 0.53 | 0.78 | 28 | empty |
| 4 | 94 | 0.45 | 0.80 | 17 | empty |
| 5 | 124 | 0.39 | 0.74 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 410 Ų buried · 3 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 Q8IVV7
- Elsewhere: RCSB PDB 7Q4Y · PDBe 7Q4Y · UniProt Q8IVV7
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