1hs7

Solution NMR

VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE

Released:
Source organism: Saccharomyces cerevisiae
Primary publication:
Vam3p structure reveals conserved and divergent properties of syntaxins.
Nat. Struct. Biol. 8 258-64 (2001)
PMID: 11224573

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Syntaxin VAM3 Chain: A
Molecule details ›
Chain: A
Length: 97 amino acids
Theoretical weight: 11.35 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q12241 (Residues: 23-119; Coverage: 34%)
Gene names: PTH1, VAM3, YOR106W, YOR3220W
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Chemical shifts: BMR4945  
Expression system: Escherichia coli BL21(DE3)