Research workbench
NMR structure of the SH3 domain from the tec protein tyrosine kinase
Analyse NMR structure of the SH3 domain from the tec protein tyrosine kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GL5
- Type
- protein
- Length
- 67 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P24604
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 67 | — | P24604 |
Compared structures
- 1GL5 · NMR structure of the SH3 domain from the Tec protein tyrosine kinase · the same entry in another collection · chain A against A, TM-score 1.00
- P24604 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase tec (P24604) · 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 P24604
- Elsewhere: RCSB PDB 1GL5 · PDBe 1GL5 · UniProt P24604
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.