Research workbench
Dimer formation through domain swapping in the crystal structure of the GRB2-SH2 ac-pyvnv complex
Analyse Dimer formation through domain swapping in the crystal structure of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FYR
- Type
- protein
- Length
- 402 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P29354, P08581
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 95 | — | P29354 |
| B, C | — | protein | 98 | — | P29354 |
| I, J, K, L | — | protein | 4 | — | P08581 |
Compared structures
- 1FYR · Dimer formation through domain swapping in the crystal structure of the GRB2-SH2 ac-pyvnv… · the same entry in another collection · chain L against L, TM-score 1.00
- P08581 · AlphaFold monomer V2.0 prediction for hepatocyte growth factor receptor (P08581) · a predicted model of the same protein · chain I against A, TM-score 0.98
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
- Every structure of UniProt P08581
- Elsewhere: RCSB PDB 1FYR · PDBe 1FYR · UniProt P29354 · UniProt P08581
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