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The structure of an anti-sigma-factor antagonist (stas) domain protein from planctomyces limnophilus.
Analyse The structure of an anti-sigma-factor antagonist (stas) domain protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3T6O
- Type
- protein
- Length
- 352 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfate TRANSPORTER/ANTISIGMA-factor antagonist stas
- UniProt
- D5SP81
- Ligands
- CL
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfate TRANSPORTER/ANTISIGMA-factor antagonist stas | protein | 118 | 41% helix, 22% strand | D5SP81 |
| B, C | Sulfate TRANSPORTER/ANTISIGMA-factor antagonist stas | protein | 117 | 42% helix, 22% strand | D5SP81 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 284 | 0.64 | 0.81 | 35 | empty |
| 2 | 273 | 0.54 | 0.76 | 23 | empty |
Interfaces
3 interfaces between chains.
- A–C · 761 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 489 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 306 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 3T6O · The Structure of an Anti-sigma-factor antagonist (STAS) domain protein from Planctomyces… · 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 D5SP81
- Elsewhere: RCSB PDB 3T6O · PDBe 3T6O · UniProt D5SP81
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