Research workbench
GID4 in complex with iglwks peptide
Analyse GID4 in complex with iglwks peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WZX
- Type
- protein
- Length
- 340 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucose-induced degradation protein 4 homolog; Ile-gly-leu-TRP-lys peptide
- UniProt
- Q8IVV7
- Ligands
- UNX
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glucose-induced degradation protein 4 homolog | protein | 165 | 13% helix, 47% strand | Q8IVV7 |
| C, D | Ile-gly-leu-TRP-lys peptide | protein | 5 | 0% helix, 60% strand | — |
Ligands and binding sites
- UNX · Unknown atom or ion · ion · 16 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 251 | 0.63 | 0.82 | 35 | empty |
| 2 | 102 | 0.41 | 0.76 | 21 | UNX |
| 3 | 77 | 0.36 | 0.76 | 21 | empty |
Interfaces
3 interfaces between chains.
- A–B · 656 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 512 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 370 Ų buried · 9 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 6WZX · PDBe 6WZX · UniProt Q8IVV7
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