1vdy

Solution NMR

NMR Structure of the hypothetical ENTH-VHS domain At3g16270 from Arabidopsis thaliana

Released:
Source organism: Arabidopsis thaliana
Entry authors: Lopez-Mendez B, Pantoja-Uceda D, Tomizawa T, Koshiba S, Kigawa T, Shirouzu M, Terada T, Inoue M, Yabuki T, Aoki M, Seki E, Matsuda T, Hirota H, Yoshida M, Tanaka A, Osanai T, Seki M, Shinozaki K, Yokoyama S, Guntert P, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein MODIFIED TRANSPORT TO THE VACUOLE 1 Chain: A
Molecule details ›
Chain: A
Length: 140 amino acids
Theoretical weight: 15.58 KDa
Source organism: Arabidopsis thaliana
Expression system: Not provided
UniProt:
  • Canonical: Q9C5H4 (Residues: 9-135; Coverage: 18%)
Gene names: At3g16270, MTV1, T02O04.23
Sequence domains: ENTH domain
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 88%
Refinement method: torsion angle dynamics
Expression system: Not provided