Research workbench
Crystal structure of EFHA2 in ca-binding state
Analyse Crystal structure of EFHA2 in ca-binding state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AGI
- Type
- protein
- Length
- 625 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium uptake protein 3, mitochondrial
- UniProt
- Q86XE3
- Ligands
- CA
- Pockets
- 9 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 59% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calcium uptake protein 3, mitochondrial | protein | 303 | 60% helix, 7% strand | Q86XE3 |
| B | Calcium uptake protein 3, mitochondrial | protein | 322 | 58% helix, 6% strand | Q86XE3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1091 | 0.83 | 0.84 | 110 | empty |
| 2 | 91 | 0.71 | 0.94 | 24 | empty |
| 3 | 113 | 0.64 | 0.88 | 27 | empty |
| 4 | 78 | 0.47 | 0.82 | 18 | empty |
| 5 | 78 | 0.43 | 0.80 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1708 Ų buried · 10 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 6AGI · PDBe 6AGI · UniProt Q86XE3
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