Research workbench
NMR study of human intestinal fatty acid binding protein
Analyse NMR study of human intestinal fatty acid binding protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IFB
- Type
- protein
- Length
- 131 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Intestinal fatty acid binding protein
- UniProt
- P12104
- Pockets
- 1 · best druggability 0.79
Structure
solution nmr · 1 distinct chain · 11% helix, 60% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Intestinal fatty acid binding protein | protein | 131 | 11% helix, 60% strand | P12104 |
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 | 213 | 0.79 | 0.92 | 41 | empty |
Compared structures
- 3IFB · NMR study of human intestinal fatty acid binding protein · the same entry in another collection · chain A against A, TM-score 1.00
- P12104 · AlphaFold monomer V2.0 prediction for fatty acid-binding protein, intestinal (P12104) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 P12104
- Elsewhere: RCSB PDB 3IFB · PDBe 3IFB · UniProt P12104
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