MolNFT v1 · #11845 · protein
Xray structure of GRB2 SH2 domain complexed with a highly affine phospho peptide
1JYQ · Growth factor receptor-bound protein 2: “Xray structure of GRB2 SH2 domain complexed with a highly affine phospho peptide”. X-ray diffraction, 1 ligand (MAZ). MolNFT v1 #11845 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1JYQ
- Type
- protein
- Length
- 198 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Growth factor receptor-bound protein 2; Maz-py-(alpha ME)PY-N-NH2 peptide inhibitor
- UniProt
- P29354
- Ligands
- MAZ
Structure
x-ray diffraction · 2 distinct chains · 16% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Growth factor receptor-bound protein 2 | protein | 96 | 17% helix, 28% strand | P29354 |
| L, H | Maz-py-(alpha ME)PY-N-NH2 peptide inhibitor | protein | 3 | 0% helix, 0% strand | — |
Ligands and binding sites
- MAZ · Formic acid 3-amino-benzyl ester · ligand · 2 copies · chains A, L, B, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 916 Ų buried · 16 hydrogen bonds · protein-protein
- A–L · 528 Ų buried · 22 hydrogen bonds · protein-protein
- B–H · 507 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified, 2 covalent (covalent ligand, nonstandard, phosphorylation).
Compared structures
- 1JYQ · Xray Structure of Grb2 SH2 Domain Complexed with a Highly Affine Phospho Peptide · 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 P29354
- Elsewhere: RCSB PDB 1JYQ · PDBe 1JYQ · UniProt P29354
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