Research workbench
Cadmium bound structure of sporosag
Analyse Cadmium bound structure of sporosag in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2X28
- Type
- protein
- Length
- 219 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sporozoite-specific sag protein
- UniProt
- Q6RUA7
- Ligands
- CD
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sporozoite-specific sag protein | protein | 219 | 6% helix, 47% strand | Q6RUA7 |
Ligands and binding sites
- CD · Cadmium ion · metal · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 120 | 0.37 | 0.73 | 17 | empty |
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 2X28 · cadmium bound structure of SporoSAG · the same entry in another collection · chain A against A, TM-score 1.00
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 Q6RUA7
- Elsewhere: RCSB PDB 2X28 · PDBe 2X28 · UniProt Q6RUA7
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