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Crystal structure of the kelch domain of human KLHL2 (mayven)
Analyse Crystal structure of the kelch domain of human KLHL2 (mayven) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XN4
- Type
- protein
- Length
- 572 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kelch-like protein 2
- UniProt
- O95198
- Ligands
- NA, SO4
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Kelch-like protein 2 | protein | 286 | 0% helix, 51% strand | O95198 |
Ligands and binding sites
- NA · Sodium ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 6 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1056 | 0.83 | 0.84 | 78 | NA |
| 2 | 377 | 0.73 | 0.84 | 36 | empty |
| 3 | 397 | 0.73 | 0.84 | 38 | empty |
Interfaces
1 interface between chains.
- A–B · 649 Ų buried · 8 hydrogen bonds · protein-protein
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 O95198
- Elsewhere: RCSB PDB 2XN4 · PDBe 2XN4 · UniProt O95198
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