Research workbench
Fully automated solution structure determination of the fes SH2 domain
Analyse Fully automated solution structure determination of the fes SH2 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DCR
- Type
- protein
- Length
- 114 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proto-oncogene tyrosine-protein kinase FES/FPS
- EC
- 2.7.1.112
- UniProt
- P07332
Structure
solution nmr · 1 distinct chain · 17% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proto-oncogene tyrosine-protein kinase FES/FPS (EC 2.7.1.112) | protein | 114 | 17% helix, 27% strand | P07332 |
Compared structures
- 2DCR · Fully automated solution structure determination of the Fes SH2 domain · the same entry in another collection · chain A against A, TM-score 1.00
- P07332 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase FES/FPS (P07332) · a predicted model of the same protein · chain A against A, TM-score 0.85
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 P07332
- Elsewhere: RCSB PDB 2DCR · PDBe 2DCR · UniProt P07332
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