3tis

X-ray diffraction
2.3Å resolution

Crystal structures of yrdA from Escherichia coli, a homologous protein of gamma-class carbonic anhydrases, show possible allosteric conformations

Released:
Source organism: Escherichia coli K-12
Primary publication:
Structures of the γ-class carbonic anhydrase homologue YrdA suggest a possible allosteric switch.
Acta Crystallogr. D Biol. Crystallogr. 68 920-6 (2012)
PMID: 22868757

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein YrdA Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 183 amino acids
Theoretical weight: 20.12 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A9W9 (Residues: 2-184; Coverage: 100%)
Gene names: JW5710, b3279, yrdA
Sequence domains: Bacterial transferase hexapeptide (six repeats)
Structure domains: Hexapeptide repeat proteins

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6C1
Spacegroup: P63
Unit cell:
a: 96.793Å b: 96.793Å c: 87.398Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.18 0.242
Expression system: Escherichia coli