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Structure of inner dysf domain of human dysferlin
Analyse Structure of inner dysf domain of human dysferlin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CAI
- Type
- protein
- Length
- 327 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dysferlin
- UniProt
- O75923
- Ligands
- PO4
- Pockets
- 4 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Dysferlin | protein | 109 | 3% helix, 37% strand | O75923 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 3 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 356 | 0.51 | 0.73 | 46 | empty |
| 2 | 67 | 0.40 | 0.80 | 18 | empty |
| 3 | 79 | 0.36 | 0.76 | 18 | empty |
| 4 | 70 | 0.36 | 0.77 | 16 | empty |
Interfaces
3 interfaces between chains.
- B–C · 510 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 501 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 487 Ų buried · 9 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 4CAI · PDBe 4CAI · UniProt O75923
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