Research workbench
Sepf-like protein from pyrococcus furiosus
Analyse Sepf-like protein from pyrococcus furiosus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZIG
- Type
- protein
- Length
- 166 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sepf-like protein
- UniProt
- I6V3Q6
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sepf-like protein | protein | 82 | 38% helix, 28% strand | I6V3Q6 |
| B | Sepf-like protein | protein | 84 | 37% helix, 25% strand | I6V3Q6 |
Interfaces
1 interface between chains.
- A–B · 140 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 3ZIG · SepF-like protein from Pyrococcus furiosus · 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 I6V3Q6
- Elsewhere: RCSB PDB 3ZIG · PDBe 3ZIG · UniProt I6V3Q6
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