Research workbench
Crystal structure of mouse apolipoprotein M
Analyse Crystal structure of mouse apolipoprotein M in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XKL
- Type
- protein
- Length
- 149 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Apolipoprotein M
- UniProt
- Q9Z1R3
- Ligands
- NA
- Pockets
- 1 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Apolipoprotein M | protein | 149 | 16% helix, 44% strand | Q9Z1R3 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A
- GOL · Glycerol · additive · chains A
- POL · N-propanol · additive · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 79 | 0.46 | 0.81 | 19 | GOL, POL |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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 Q9Z1R3
- Elsewhere: RCSB PDB 2XKL · PDBe 2XKL · UniProt Q9Z1R3
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