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Crystal structure of FIP1 with gsh
Analyse Crystal structure of FIP1 with gsh in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ECS
- Type
- protein
- Length
- 428 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase U20
- EC
- 2.5.1.18
- UniProt
- Q8L7C9
- Ligands
- GSH
- Pockets
- 7 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutathione S-transferase U20 (EC 2.5.1.18) | protein | 214 | 62% helix, 8% strand | Q8L7C9 |
Ligands and binding sites
- GSH · Glutathione · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 183 | 0.48 | 0.76 | 22 | GSH |
| 2 | 163 | 0.45 | 0.75 | 23 | GSH |
| 3 | 187 | 0.45 | 0.74 | 23 | empty |
| 4 | 92 | 0.42 | 0.78 | 17 | empty |
| 5 | 144 | 0.41 | 0.74 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 399 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 Q8L7C9
- Elsewhere: RCSB PDB 5ECS · PDBe 5ECS · UniProt Q8L7C9
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