› 2lns

Solution NMR

Solution structure of AGR2 residues 41-175

Released:
DOI: 10.2210/pdb2lns/pdb
PDB entry 2lns coloured by chain, ensemble of 10 models, front view.
PDB entry 2lns coloured by chain, ensemble of 10 models, side view.
PDB entry 2lns coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Metastasis-promoting anterior gradient 2 protein has a dimeric thioredoxin fold structure and a role in cell adhesion.
Patel P, Clarke C, Barraclough DL, Jowitt TA, Rudland PS, Barraclough R, Lian LY
J Mol Biol 425 929-43 (2013)
PMID: 23274113

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132100 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Anterior gradient protein 2 homolog Chains: A, B
Molecule details ›
Chains: A, B
Length: 140 amino acids
Theoretical weight: 16.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95994 (Residues: 41-175; Coverage: 87%)
Gene names: AG2, AGR2, UNQ515/PRO1030
Sequence domains: Thioredoxin-like
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 24%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Mechanisms of anterior gradient-2 regulation and function in cancer.
Brychtova et al. (2015)
8 more

10 mentions without citation

Secretion of pro-oncogenic AGR2 protein in cancer.
Moidu et al. (2020)
9 more