Research workbench
Crystal structure of the N-terminal SH2 domain of mouse phospholipase C-gamma 2
Analyse Crystal structure of the N-terminal SH2 domain of mouse phospholipase C-gamma 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DX0
- Type
- protein
- Length
- 212 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8CIH5
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 117 | — | Q8CIH5 |
| B | — | protein | 95 | — | Q8CIH5 |
Compared structures
- 2DX0 · Crystal structure of the N-terminal SH2 domain of mouse phospholipase C-gamma 2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q8CIH5 · AlphaFold monomer V2.0 prediction for 1-phosphatidylinositol 4,5-bisphosphate… · a predicted model of the same protein · chain B against A, TM-score 0.80
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 Q8CIH5
- Elsewhere: RCSB PDB 2DX0 · PDBe 2DX0 · UniProt Q8CIH5
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