The helix-hinge-helix structural motif in human apolipoprotein a-I determined by NMR spectroscopy, 1 structure. Determined by solution NMR. Released 23 Jul 1997.
Explore 1GW3 in 3D Show helices and sheets RCSB PDB PDBe
1GW3 contains 3 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-21 | 8 | |
| α-helix | 27-35 | 9 | |
| α-helix | 36-38 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apoa-I | A | protein | 46 | Homo sapiens | P02647 (AlphaFold model) |
>1GW3_1 APOA-I (chains A) SPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGA
The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy. Wang, G., Sparrow, J.T., Cushley, R.J. Biochemistry (1997) 36:13657-13666. DOI 10.1021/bi971151q · PubMed
Other PDB entries of the same protein (UniProt P02647 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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