Research workbench
GRB2 SH2 complexed with a ptyr-AC6CN-asn tripeptide
Analyse GRB2 SH2 complexed with a ptyr-AC6CN-asn tripeptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4P9V
- Type
- protein
- Length
- 103 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Growth factor receptor-bound protein 2; Phq-ptr-02K-asn-NH2
- UniProt
- P62993
- Ligands
- PHQ, NH2, CL
Structure
x-ray diffraction · 2 distinct chains · 16% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Growth factor receptor-bound protein 2 | protein | 100 | 16% helix, 27% strand | P62993 |
| B | Phq-ptr-02K-asn-NH2 | protein | 3 | 0% helix, 0% strand | — |
Ligands and binding sites
- PHQ · benzyl chlorocarbonate · ligand · chains A, B
- NH2 · Amino group · ion · chains A, B
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 396 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified, 1 covalent (covalent ligand, nonstandard, phosphorylation).
Compared structures
- 4P9V · Grb2 SH2 complexed with a pTyr-Ac6cN-Asn tripeptide · 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 0.95
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 4P9V · PDBe 4P9V · UniProt P62993
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