Research workbench
Solution NMR structure of the shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor, minimized average structure
Analyse Solution NMR structure of the shc SH2 domain complexed with a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TCE
- Type
- protein
- Length
- 121 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P29353, P20963
Structure
solution nmr · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 107 | — | P29353 |
| B | — | protein | 14 | — | P20963 |
Compared structures
- 1TCE · Solution NMR structure of the shc SH2 domain complexed with a tyrosine-phosphorylated… · the same entry in another collection · chain A against A, TM-score 1.00
- P29353 · AlphaFold monomer V2.0 prediction for shc-transforming protein 1 (P29353) · a predicted model of the same protein · chain A against A, TM-score 0.87
- P20963 · P20963 · a predicted model of the same protein · chain B against A, TM-score 0.21
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 P29353
- Every structure of UniProt P20963
- Elsewhere: RCSB PDB 1TCE · PDBe 1TCE · UniProt P29353 · UniProt P20963
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