3ph9

X-ray diffraction
1.83Å resolution

Crystal structure of the human anterior gradient protein 3

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of human anterior gradient protein 3.
Acta Crystallogr F Struct Biol Commun 74 425-430 (2018)
PMID: 29969106

Function and Biology Details

Reaction catalysed:
Catalyzes the rearrangement of -S-S- bonds in proteins
Biochemical function:
Biological process:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-186198 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Anterior gradient protein 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 151 amino acids
Theoretical weight: 17.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8TD06 (Residues: 24-166; Coverage: 99%)
Gene names: AGR3, BCMP11, PDIA18, UNQ642/PRO1272
Sequence domains: Thioredoxin-like
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 33.29Å b: 71.45Å c: 59.81Å
α: 90° β: 97.72° γ: 90°
R-values:
R R work R free
0.18 0.177 0.233
Expression system: Escherichia coli BL21(DE3)