MolNFT v1 · #143123 · protein
The crystal structure of human FABP3
6AQ1 · Fatty acid-binding protein, heart: “The crystal structure of human FABP3”. X-ray diffraction, 2 ligands (PLM, SO4), 3 pockets (best druggability 0.82). MolNFT v1 #143123 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6AQ1
- Type
- protein
- Length
- 268 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty acid-binding protein, heart
- UniProt
- P05413
- Ligands
- PLM, SO4
- Pockets
- 3 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fatty acid-binding protein, heart | protein | 134 | 14% helix, 58% strand | P05413 |
Ligands and binding sites
- PLM · Palmitic acid · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 4 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 | 497 | 0.82 | 0.89 | 57 | SO4, PLM |
| 2 | 318 | 0.82 | 0.92 | 34 | PLM |
| 3 | 124 | 0.38 | 0.73 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 487 Ų buried · 6 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 P05413
- Elsewhere: RCSB PDB 6AQ1 · PDBe 6AQ1 · UniProt P05413
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