Research workbench
NMR structure of the apo V-src SH2 domain
Analyse NMR structure of the apo V-src SH2 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JYQ
- Type
- protein
- Length
- 106 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase transforming protein src
- EC
- 2.7.10.2
- UniProt
- P63185
Structure
solution nmr · 1 distinct chain · 15% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase transforming protein src (EC 2.7.10.2) | protein | 106 | 15% helix, 33% strand | P63185 |
Compared structures
- 2JYQ · NMR structure of the apo v-Src SH2 domain · the same entry in another collection · chain A against A, TM-score 1.00
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 P63185
- Elsewhere: RCSB PDB 2JYQ · PDBe 2JYQ · UniProt P63185
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