Research workbench
Crystal structure of EFHA2 in apo state
Analyse Crystal structure of EFHA2 in apo state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AGJ
- Type
- protein
- Length
- 624 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium uptake protein 3, mitochondrial
- UniProt
- Q86XE3
- Pockets
- 10 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 62% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calcium uptake protein 3, mitochondrial | protein | 309 | 61% helix, 7% strand | Q86XE3 |
| B | Calcium uptake protein 3, mitochondrial | protein | 315 | 64% helix, 7% strand | Q86XE3 |
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 260 | 0.75 | 0.88 | 37 | empty |
| 2 | 266 | 0.73 | 0.87 | 34 | empty |
| 3 | 490 | 0.69 | 0.80 | 48 | empty |
| 4 | 295 | 0.67 | 0.82 | 27 | empty |
| 5 | 120 | 0.57 | 0.84 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1512 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 Q86XE3
- Elsewhere: RCSB PDB 6AGJ · PDBe 6AGJ · UniProt Q86XE3
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