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Crystal Structure of domain swapped human Nck SH3.1, 1.01A, monoclinic
Analyse Crystal Structure of domain swapped human Nck SH3.1, 1.01A, monoclinic in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5QU3
- Type
- protein
- Length
- 113 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.02
- Source
- Homo sapiens
- Molecule
- Cytoplasmic protein NCK1
- UniProt
- P16333
Structure
x-ray diffraction · resolution 1.02 · 2 distinct chains · 5% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytoplasmic protein NCK1 | protein | 57 | 5% helix, 42% strand | P16333 |
| B | Cytoplasmic protein NCK1 | protein | 56 | 5% helix, 43% strand | P16333 |
Interfaces
1 interface between chains.
- A–B · 2199 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 5QU3 · Crystal structure of domain swapped human nck SH3.1, 1.01A, monoclinic · the same entry in another collection · chain A against A, TM-score 1.00
- P16333 · AlphaFold monomer V2.0 prediction for cytoplasmic protein NCK1 (P16333) · a predicted model of the same protein · chain B against A, TM-score 0.57
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 P16333
- Elsewhere: RCSB PDB 5QU3 · PDBe 5QU3 · UniProt P16333
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