Research workbench
The structure of pyrococcus furiosus sfsa in complex with CA2+
Analyse The structure of pyrococcus furiosus sfsa in complex with CA2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DA2
- Type
- protein
- Length
- 462 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sugar fermentation stimulation protein homolog
- UniProt
- Q8U1K8
- Ligands
- CA
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Sugar fermentation stimulation protein homolog | protein | 231 | 19% helix, 44% strand | Q8U1K8 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 874 | 0.75 | 0.79 | 82 | CA |
| 2 | 286 | 0.63 | 0.81 | 39 | CA |
| 3 | 100 | 0.34 | 0.73 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 566 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4DA2 · The structure of Pyrococcus Furiosus SfsA in complex with Ca2+ · the same entry in another collection · chain A against A, TM-score 1.00
- Q8U1K8 · AlphaFold monomer V2.0 prediction for sugar fermentation stimulation protein homolog… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q8U1K8
- Elsewhere: RCSB PDB 4DA2 · PDBe 4DA2 · UniProt Q8U1K8
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