MolNFT v1 · #145076 · protein
GID4 in complex with a tetrapeptide
6CDC · Glucose-induced degradation protein 4 homolog: “GID4 in complex with a tetrapeptide”. X-ray diffraction, 1 ligand (UNX), 1 pocket (best druggability 0.37). MolNFT v1 #145076 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6CDC
- Type
- protein
- Length
- 167 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucose-induced degradation protein 4 homolog; Tetrapeptide pglw
- UniProt
- Q8IVV7
- Ligands
- UNX
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucose-induced degradation protein 4 homolog | protein | 163 | 12% helix, 48% strand | Q8IVV7 |
| C | Tetrapeptide pglw | protein | 4 | 0% helix, 50% strand | — |
Ligands and binding sites
- UNX · Unknown atom or ion · ion · 7 copies · chains A, C
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 | 93 | 0.37 | 0.75 | 23 | empty |
Interfaces
1 interface between chains.
- A–C · 493 Ų buried · 13 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 6CDC · PDBe 6CDC · UniProt Q8IVV7
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