Research workbench
Crystal structure of a proteolytically cleaved, amino terminal domain of apolipoprotein E3
Analyse Crystal structure of a proteolytically cleaved, amino terminal domain of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V7M
- Type
- protein
- Length
- 147 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Homo sapiens
- Molecule
- Apolipoprotein E
- UniProt
- P02649
- Ligands
- PO4
Structure
x-ray diffraction · resolution 2 · 2 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Apolipoprotein E | protein | 64 | 75% helix, 0% strand | P02649 |
| B | Apolipoprotein E | protein | 83 | 83% helix, 0% strand | P02649 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1588 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 6V7M · Crystal structure of a proteolytically cleaved, amino terminal domain of apolipoprotein E3 · the same entry in another collection · chain A against A, TM-score 1.00
- P02649 · AlphaFold monomer V2.0 prediction for apolipoprotein E (P02649) · a predicted model of the same protein · chain B against A, TM-score 0.93
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 P02649
- Elsewhere: RCSB PDB 6V7M · PDBe 6V7M · UniProt P02649
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