Research workbench
Structure of sulp transporter stas domain from vibrio cholerae refined to 1.9 ångström resolution
Analyse Structure of sulp transporter stas domain from vibrio cholerae refined to 1.9… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DGH
- Type
- protein
- Length
- 256 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfate permease family protein
- UniProt
- Q9KN88
- Ligands
- K, IOD
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Sulfate permease family protein | protein | 128 | 53% helix, 13% strand | Q9KN88 |
Ligands and binding sites
- K · Potassium ion · metal · chains A
- IOD · Iodide ion · ion · 15 copies · chains A, B
- GOL · Glycerol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 395 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 4DGH · Structure of SulP Transporter STAS Domain from Vibrio Cholerae Refined to 1.9 Angstrom… · 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 Q9KN88
- Elsewhere: RCSB PDB 4DGH · PDBe 4DGH · UniProt Q9KN88
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