Research workbench
Stage V sporolation protein S (spovs) from thermus thermophilus
Analyse Stage V sporolation protein S (spovs) from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EH1
- Type
- protein
- Length
- 177 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Stage V sporulation protein S (spovs) related protein
- UniProt
- Q5SK02
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Stage V sporulation protein S (spovs) related protein | protein | 88 | 40% helix, 43% strand | Q5SK02 |
| B | Stage V sporulation protein S (spovs) related protein | protein | 89 | 39% helix, 38% strand | Q5SK02 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 392 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 2EH1 · Stage V Sporolation Protein S (SpoVS) from Thermus thermophilus · 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 Q5SK02
- Elsewhere: RCSB PDB 2EH1 · PDBe 2EH1 · UniProt Q5SK02
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