Research workbench
Structural basis for the specific interaction of lysine- containing proline-rich peptides with the N-terminal SH3 domain of C-crk
Analyse Structural basis for the specific interaction of lysine- containing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CKA
- Type
- protein
- Length
- 66 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q64010
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 57 | — | Q64010 |
| B | — | protein | 9 | — | — |
Compared structures
- 1CKA · Structural basis for the specific interaction of lysine-containing proline-rich peptides… · the same entry in another collection · chain A against A, TM-score 1.00
- Q64010 · AlphaFold monomer V2.0 prediction for adapter molecule crk (Q64010) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q64010
- Elsewhere: RCSB PDB 1CKA · PDBe 1CKA · UniProt Q64010
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