6vxe

X-ray diffraction
2.46Å resolution

Crystal structure of hydroxyproline dehydratase (HypD) from Clostridioides difficile with substrate trans-4-hydroxy-L-proline bound

Released:

Function and Biology Details

Reaction catalysed:
Trans-4-hydroxy-L-proline = (S)-1-pyrroline-5-carboxylate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trans-4-hydroxy-L-proline dehydratase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 809 amino acids
Theoretical weight: 91.46 KDa
Source organism: Clostridioides difficile 70-100-2010
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A031WDE4 (Residues: 1-789; Coverage: 100%)
Gene names: BGU81_07860, BN1095_640054, BN1096_740112, BN1097_360077, SAMEA3375004_02654, csdB_2, pflD
Sequence domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 100.346Å b: 341.655Å c: 122.605Å
α: 90° β: 107.14° γ: 90°
R-values:
R R work R free
0.196 0.194 0.23
Expression system: Escherichia coli BL21(DE3)