Research workbench
Fabp ground state captured by xfels
Analyse Fabp ground state captured by xfels in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DZE
- Type
- protein
- Length
- 258 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty acid-binding protein, liver
- UniProt
- P07148
- Ligands
- PLM
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fatty acid-binding protein, liver | protein | 129 | 12% helix, 59% strand | P07148 |
Ligands and binding sites
- PLM · Palmitic acid · ligand · 2 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 235 | 0.83 | 0.95 | 39 | PLM |
| 2 | 241 | 0.83 | 0.95 | 42 | PLM |
| 3 | 54 | 0.33 | 0.77 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 701 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
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 P07148
- Elsewhere: RCSB PDB 7DZE · PDBe 7DZE · UniProt P07148
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