Research workbench
Global structure and dynamics of human apolipoprotein cii in complex with micelles: evidence for increased mobility of the helix involvved in the activation of lipoprotein lipase.
Analyse Global structure and dynamics of human apolipoprotein cii in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1O8T
- Type
- protein
- Length
- 79 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P02655
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 79 | — | P02655 |
Compared structures
- 1O8T · Global Structure and Dynamics of Human Apolipoprotein CII in Complex with Micelles… · the same entry in another collection · chain A against A, TM-score 1.00
- P02655 · AlphaFold monomer V2.0 prediction for apolipoprotein C-II (P02655) · a predicted model of the same protein · chain A against A, TM-score 0.45
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 P02655
- Elsewhere: RCSB PDB 1O8T · PDBe 1O8T · UniProt P02655
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