Research workbench
GRB2-SH2 domain in complex with cyclo-[N-alpha-acetyl-L-thi alysyl-O-phosphotyrosyl-valyl-asparagyl-valyl-prolyl] (PKF273-791)
Analyse GRB2-SH2 domain in complex with cyclo-[N-alpha-acetyl-L-thi… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BM2
- Type
- protein
- Length
- 104 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (growth factor receptor bound protein 2); Protein (PKF273-791)
- UniProt
- P29354
- Ligands
- ACE
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (growth factor receptor bound protein 2) | protein | 98 | 19% helix, 29% strand | P29354 |
| L | Protein (PKF273-791) | protein | 6 | 0% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–L · 421 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified, 1 covalent (covalent ligand, nonstandard, phosphorylation).
Compared structures
- 1BM2 · GRB2-SH2 domain in complex with cyclo-[N-alpha-acetyl-L-thi… · 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 1BM2 · PDBe 1BM2 · UniProt P29354
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.