Research workbench
Critical structural role for the pH and C1 domains of the VAV1 exchange factor
Analyse Critical structural role for the pH and C1 domains of the VAV1 exchange factor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VRW
- Type
- protein
- Length
- 544 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P63000, P27870
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 177 | — | P63000 |
| B | — | protein | 367 | — | P27870 |
Compared structures
- 2VRW · Critical structural role for the PH and C1 domains of the Vav1 exchange factor · the same entry in another collection · chain A against A, TM-score 1.00
- P63000 · AlphaFold monomer V2.0 prediction for RAS-related C3 botulinum toxin substrate 1 (P63000) · a predicted model of the same protein · chain A against A, TM-score 0.94
- P27870 · AlphaFold monomer V2.0 prediction for proto-oncogene vav (P27870) · a predicted model of the same protein · chain B against A, TM-score 0.93
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 P63000
- Every structure of UniProt P27870
- Elsewhere: RCSB PDB 2VRW · PDBe 2VRW · UniProt P63000 · UniProt P27870
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