Research workbench
Computationally designed two-component self-assembling tetrahedral cage, T33-21, crystallized in space group F4132
Analyse Computationally designed two-component self-assembling tetrahedral cage… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NWQ
- Type
- protein
- Length
- 269 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative uncharacterized protein PH0671; Uncharacterized protein
- UniProt
- O58404, Q9I2D8
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative uncharacterized protein PH0671 | protein | 148 | 74% helix, 1% strand | O58404 |
| B | Uncharacterized protein | protein | 121 | 28% helix, 32% strand | Q9I2D8 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 11 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 17 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4NWQ · Computationally Designed Two-Component Self-Assembling Tetrahedral Cage, T33-21… · 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 O58404
- Every structure of UniProt Q9I2D8
- Elsewhere: RCSB PDB 4NWQ · PDBe 4NWQ · UniProt O58404 · UniProt Q9I2D8
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