Research workbench
Xray structure of GRB2 SH2 domain complexed with a phosphorylated peptide
Analyse Xray structure of GRB2 SH2 domain complexed with a phosphorylated peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JYR
- Type
- protein
- Length
- 105 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Growth factor receptor-bound protein 2; Peptide: pspyvnvqn
- UniProt
- P62993
Structure
x-ray diffraction · 2 distinct chains · 15% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Growth factor receptor-bound protein 2 | protein | 96 | 17% helix, 28% strand | P62993 |
| L | Peptide: pspyvnvqn | protein | 9 | 0% helix, 0% strand | — |
Interfaces
1 interface between chains.
- A–L · 455 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 1JYR · Xray Structure of Grb2 SH2 Domain Complexed with a Phosphorylated Peptide · the same entry in another collection · chain A against A, TM-score 1.00
- P62993 · AlphaFold monomer V2.0 prediction for growth factor receptor-bound protein 2 (P62993) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P62993
- Elsewhere: RCSB PDB 1JYR · PDBe 1JYR · UniProt P62993
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