Research workbench
NMR study of the SH3 domain from BRUTON'S tyrosine kinase, 20 structures
Analyse NMR study of the SH3 domain from BRUTON'S tyrosine kinase, 20 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QLY
- Type
- protein
- Length
- 58 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase btk
- EC
- 2.7.1.112
- UniProt
- Q06187
Structure
solution nmr · 1 distinct chain · 0% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase btk (EC 2.7.1.112) | protein | 58 | 0% helix, 34% strand | Q06187 |
Compared structures
- 1QLY · NMR Study of the SH3 Domain From Bruton's Tyrosine Kinase, 20 Structures · the same entry in another collection · chain A against A, TM-score 1.00
- Q06187 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase btk (Q06187) · 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 Q06187
- Elsewhere: RCSB PDB 1QLY · PDBe 1QLY · UniProt Q06187
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