Function and Biology Details
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- RNA recognition motif domain
- Nucleotide-binding alpha-beta plait domain superfamily
- RNA-binding domain superfamily
- Ribonucleoprotein PTB-binding 1, RNA recognition motif 3
- Ribonucleoprotein PTB-binding 1, RNA recognition motif 1
- Vinculin
- Alpha-catenin/vinculin-like superfamily
- Vinculin/alpha-catenin
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Vinculin and Ribonucleoprotein PTB-binding 1 (preferred)
PDBe Complex ID:
PDB-CPX-148324 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Vinculin
Molecule details ›
Chains: A, C
Length: 188 amino acids
Theoretical weight: 21.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Vinculin family
Structure domains: Alpha-catenin/vinculin-like
Length: 188 amino acids
Theoretical weight: 21.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P18206 (Residues: 944-1134; Coverage: 17%)
Sequence domains: Vinculin family
Structure domains: Alpha-catenin/vinculin-like
Ribonucleoprotein PTB-binding 1
Molecule details ›
Chains: B, D
Length: 283 amino acids
Theoretical weight: 31.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: RNA recognition motif
Structure domains: Alpha-Beta Plaits
Length: 283 amino acids
Theoretical weight: 31.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q8IY67 (Residues: 39-321; Coverage: 47%)
Sequence domains: RNA recognition motif
Structure domains: Alpha-Beta Plaits
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 22-BM
Spacegroup:
P212121
Expression system: Escherichia coli
