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The dimerization domain of LAP2ALPHA
Analyse The dimerization domain of LAP2ALPHA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V0X
- Type
- protein
- Length
- 400 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lamina-associated polypeptide 2 isoforms ALPHA/ZETA
- UniProt
- Q61033
- Pockets
- 5 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 65% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lamina-associated polypeptide 2 isoforms ALPHA/ZETA | protein | 195 | 65% helix, 2% strand | Q61033 |
| B | Lamina-associated polypeptide 2 isoforms ALPHA/ZETA | protein | 205 | 64% helix, 1% strand | Q61033 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.58 | 0.85 | 24 | empty |
| 2 | 108 | 0.39 | 0.75 | 18 | empty |
| 3 | 62 | 0.32 | 0.76 | 13 | empty |
| 4 | 52 | 0.27 | 0.74 | 12 | empty |
| 5 | 56 | 0.26 | 0.72 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 4564 Ų buried · 39 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
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 Q61033
- Elsewhere: RCSB PDB 2V0X · PDBe 2V0X · UniProt Q61033
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