Research workbench
Structure of sulp transporter stas domain from wolinella succinogenes refined to 1.6 ångström resolution
Analyse Structure of sulp transporter stas domain from wolinella succinogenes refined… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DGF
- Type
- protein
- Length
- 247 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfate transporter sulfate transporter family protein
- UniProt
- Q7M9V0
- Ligands
- CL
- Pockets
- 2 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfate transporter sulfate transporter family protein | protein | 122 | 51% helix, 15% strand | Q7M9V0 |
| B | Sulfate transporter sulfate transporter family protein | protein | 125 | 48% helix, 14% strand | Q7M9V0 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
- FMT · Formic acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.47 | 0.80 | 23 | empty |
| 2 | 137 | 0.41 | 0.75 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 703 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 4DGF · Structure of SulP Transporter STAS Domain from Wolinella Succinogenes Refined to 1.6… · 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 Q7M9V0
- Elsewhere: RCSB PDB 4DGF · PDBe 4DGF · UniProt Q7M9V0
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