3tio

X-ray diffraction
1.41Å resolution

Crystal structures of yrdA from Escherichia coli, a homologous protein of gamma-class carbonic anhydrase, 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)
Assembly name:
PDBe Complex ID:
PDB-CPX-141938 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein YrdA Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
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

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P21
Unit cell:
a: 55.976Å b: 84.384Å c: 97.758Å
α: 90° β: 93.18° γ: 90°
R-values:
R R work R free
0.193 0.193 0.21
Expression system: Escherichia coli