Research workbench
Barium derivative of human lfabp
Analyse Barium derivative of human lfabp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VG6
- Type
- protein
- Length
- 130 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty acid-binding protein, liver
- UniProt
- P07148
- Ligands
- PLM, BA, IOD
- Pockets
- 1 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fatty acid-binding protein, liver | protein | 130 | 12% helix, 58% strand | P07148 |
Ligands and binding sites
- PLM · Palmitic acid · ligand · 2 copies · chains A
- BA · Barium ion · metal · 2 copies · chains A
- IOD · Iodide ion · ion · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 400 | 0.84 | 0.91 | 48 | PLM, IOD |
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 3VG6 · PDBe 3VG6 · UniProt P07148
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