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Structure of 206-gvvtse-211, the steric zipper that supports the self- association of P. stuartii omp-PST1 into dimers of trimers
Analyse Structure of 206-gvvtse-211, the steric zipper that supports the self… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5N9I
- Type
- protein
- Length
- 24 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Porin 1
- UniProt
- E3U904
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Porin 1 | protein | 6 | 0% helix, 0% strand | E3U904 |
Interfaces
5 interfaces between chains.
- B–C · 115 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 104 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 87 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 39 Ų buried · 1 hydrogen bond · protein-protein
- C–D · 37 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 5N9I · Structure of 206-gvvtse-211, the steric zipper that supports the self-association of P.… · 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 E3U904
- Elsewhere: RCSB PDB 5N9I · PDBe 5N9I · UniProt E3U904
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