Research workbench
Solution structure of the VAV1 SH2 domain complexed with a syk-derived singly phosphorylated peptide
Analyse Solution structure of the VAV1 SH2 domain complexed with a syk-derived singly… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MC1
- Type
- protein
- Length
- 120 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proto-oncogene vav; Tyrosine-protein kinase syk
- UniProt
- P15498, P48025
Structure
solution nmr · 2 distinct chains · 20% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proto-oncogene vav | protein | 107 | 22% helix, 26% strand | P15498 |
| B | Tyrosine-protein kinase syk | protein | 13 | 0% helix, 0% strand | P48025 |
Interfaces
1 interface between chains.
- A–B · 697 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 2MC1 · Solution structure of the Vav1 SH2 domain complexed with a Syk-derived singly… · the same entry in another collection · chain A against A, TM-score 1.00
- P15498 · AlphaFold monomer V2.0 prediction for proto-oncogene vav (P15498) · a predicted model of the same protein · chain A against A, TM-score 0.86
- P48025 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase syk (P48025) · a predicted model of the same protein · chain B against A, TM-score 0.35
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 P15498
- Every structure of UniProt P48025
- Elsewhere: RCSB PDB 2MC1 · PDBe 2MC1 · UniProt P15498 · UniProt P48025
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