Research workbench
Crystal structure of the monomeric human nck SH3.1 domain, triclinic, 1.08A
Analyse Crystal structure of the monomeric human nck SH3.1 domain, triclinic, 1.08A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5QU1
- Type
- protein
- Length
- 112 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytoplasmic protein NCK1
- UniProt
- P16333
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cytoplasmic protein NCK1 | protein | 56 | 5% helix, 46% strand | P16333 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 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 · 550 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 5QU1 · Crystal Structure of the monomeric human Nck SH3.1 domain, triclinic, 1.08A · 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 A against A, TM-score 0.97
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 5QU1 · PDBe 5QU1 · UniProt P16333
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