Research workbench
N-terminal SH3 domain of GRB2 protein
Analyse N-terminal SH3 domain of GRB2 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SDF
- Type
- protein
- Length
- 119 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Growth factor receptor-bound protein 2
- UniProt
- P62993
- Ligands
- CL
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Growth factor receptor-bound protein 2 | protein | 61 | 5% helix, 44% strand | P62993 |
| B | Growth factor receptor-bound protein 2 | protein | 58 | 5% helix, 47% strand | P62993 |
Ligands and binding sites
- CL · Chloride ion · ion · 3 copies · chains A, B
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.39 | 0.77 | 13 | MPD |
Interfaces
1 interface between chains.
- A–B · 371 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
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 6SDF · PDBe 6SDF · UniProt P62993
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