Research workbench
2.2 ångström crystal structure of C terminal truncated human apolipoprotein a-I reveals the assembly of HDL by dimerization.
Analyse 2.2 ångström crystal structure of C terminal truncated human apolipoprotein a-I… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3R2P
- Type
- protein
- Length
- 180 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P02647
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 180 | — | P02647 |
Compared structures
- 3R2P · 2.2 Angstrom Crystal Structure of C Terminal Truncated Human Apolipoprotein A-I Reveals… · 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 0.45
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 P02647
- Elsewhere: RCSB PDB 3R2P · PDBe 3R2P · UniProt P02647
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