Research workbench
NMR solution structure of the N-terminal SH3 domain of human nckalpha
Analyse NMR solution structure of the N-terminal SH3 domain of human nckalpha in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JW4
- Type
- protein
- Length
- 72 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytoplasmic protein NCK1
- UniProt
- P16333
Structure
solution nmr · 1 distinct chain · 0% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytoplasmic protein NCK1 | protein | 72 | 0% helix, 28% strand | P16333 |
Compared structures
- 2JW4 · NMR solution structure of the N-terminal SH3 domain of human Nckalpha · 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 0.76
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 2JW4 · PDBe 2JW4 · UniProt P16333
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