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Crystal structure of CURCULIN1 homodimer
Analyse Crystal structure of CURCULIN1 homodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DPF
- Type
- protein
- Length
- 444 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Curculin
- UniProt
- P19667
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Curculin | protein | 111 | 0% helix, 45% strand | P19667 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.36 | 0.76 | 18 | empty |
| 2 | 76 | 0.35 | 0.76 | 18 | empty |
| 3 | 75 | 0.34 | 0.76 | 15 | empty |
Interfaces
2 interfaces between chains.
- C–D · 1337 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 1306 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
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 P19667
- Elsewhere: RCSB PDB 2DPF · PDBe 2DPF · UniProt P19667
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