Research workbench
The helix-hinge-helix structural motif in human apolipoprotein a-I determined by NMR spectroscopy, 1 structure
Analyse The helix-hinge-helix structural motif in human apolipoprotein a-I determined… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GW3
- Type
- protein
- Length
- 46 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Apoa-I
- UniProt
- P02647
Structure
solution nmr · 1 distinct chain · 43% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Apoa-I | protein | 46 | 43% helix, 0% strand | P02647 |
Compared structures
- 1GW3 · The helix-hinge-helix structural motif in human apolipoprotein a-I determined by NMR… · the same entry in another collection · chain A against A, TM-score 1.00
- P02647 · AlphaFold monomer V2.0 prediction for apolipoprotein a-I (P02647) · a predicted model of the same protein · chain A against A, TM-score 0.49
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 P02647
- Elsewhere: RCSB PDB 1GW3 · PDBe 1GW3 · UniProt P02647
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