MolNFT v1 · #145055 · protein
Selenomethionyl derivative of a GID4 fragment
6CCR · Glucose-induced degradation protein 4 homolog: “Selenomethionyl derivative of a GID4 fragment”. X-ray diffraction, 1 ligand (UNX), 2 pockets (best druggability 0.55). MolNFT v1 #145055 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6CCR
- Type
- protein
- Length
- 186 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucose-induced degradation protein 4 homolog
- UniProt
- Q8IVV7
- Ligands
- UNX
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucose-induced degradation protein 4 homolog | protein | 186 | 16% helix, 42% strand | Q8IVV7 |
Ligands and binding sites
- UNX · Unknown atom or ion · ion · 36 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 166 | 0.55 | 0.80 | 24 | empty |
| 2 | 186 | 0.52 | 0.78 | 28 | UNX |
Modifications
Observed in the structure: 1 modified (engineered).
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 6CCR · PDBe 6CCR · UniProt Q8IVV7
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