Research workbench
Fatty acid and retinol binding protein na-far-1 from necator americanus
Analyse Fatty acid and retinol binding protein na-far-1 from necator americanus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XCP
- Type
- protein
- Length
- 155 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nematode fatty acid retinoid binding protein
- UniProt
- W2SRJ3
- Ligands
- PLM
- Pockets
- 1 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nematode fatty acid retinoid binding protein | protein | 155 | 78% helix, 0% strand | W2SRJ3 |
Ligands and binding sites
- PLM · Palmitic acid · ligand · 2 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 | 933 | 0.85 | 0.85 | 61 | PLM |
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 4XCP · Fatty Acid and Retinol binding protein Na-FAR-1 from Necator americanus · the same entry in another collection · chain A against A, TM-score 1.00
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 W2SRJ3
- Elsewhere: RCSB PDB 4XCP · PDBe 4XCP · UniProt W2SRJ3
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