MolNFT v1 · #178874 · protein
Calcium-bound C2A domain from human dysferlin
7JOF · Isoform 6 of dysferlin: “Calcium-bound C2A domain from human dysferlin”. X-ray diffraction, 1 ligand (CA), 4 pockets (best druggability 0.70). MolNFT v1 #178874 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7JOF
- Type
- protein
- Length
- 496 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoform 6 of dysferlin
- UniProt
- O75923
- Ligands
- CA
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 4 distinct chains · 3% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isoform 6 of dysferlin | protein | 122 | 2% helix, 57% strand | O75923 |
| B | Isoform 6 of dysferlin | protein | 126 | 3% helix, 54% strand | O75923 |
| C | Isoform 6 of dysferlin | protein | 122 | 3% helix, 57% strand | O75923 |
| D | Isoform 6 of dysferlin | protein | 126 | 3% helix, 56% strand | O75923 |
Ligands and binding sites
- CA · Calcium ion · metal · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1117 | 0.70 | 0.74 | 116 | empty |
| 2 | 291 | 0.52 | 0.74 | 28 | empty |
| 3 | 91 | 0.43 | 0.78 | 19 | empty |
| 4 | 63 | 0.41 | 0.80 | 10 | empty |
Interfaces
4 interfaces between chains.
- B–C · 455 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 295 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 184 Ų buried · 0 hydrogen bonds · protein-protein
- C–D · 136 Ų buried · 3 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 O75923
- Elsewhere: RCSB PDB 7JOF · PDBe 7JOF · UniProt O75923
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