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Crystal structure of C171A/V236A Mutant of N-carbamyl-D-amino acid amidohydrolase complexed with N-carbamyl-D-valine

X-ray diffraction
1.9Å resolution
PDB entry 1uf7 coloured by chain, front view.
PDB entry 1uf7 coloured by chain, side view.
PDB entry 1uf7 coloured by chain, top view.
Source organism: Agrobacterium sp.
Assembly composition:
homo tetramer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: N-carbamoyl-D-amino acid hydrolase
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Multimeric state: homo tetramer
Accessible surface area: 38371.04 Å2
Buried surface area: 14603.52 Å2
Dissociation area: 1,933.87 Å2
Dissociation energy (ΔGdiss): 1.76 kcal/mol
Dissociation entropy (TΔSdiss): 15.06 kcal/mol
Symmetry number: 4
PDBe Complex ID: PDB-CPX-157995

Macromolecules

N-carbamoyl-D-amino acid hydrolase
Chains: A, B
Length: 303 amino acids
Theoretical weight: 34.14 KDa
Source organism: Agrobacterium sp.
Expression system: Escherichia coli
UniProt:
  • Canonical: P60327 (Residues: 2-304; Coverage: 100%)
Pfam: Carbon-nitrogen hydrolase
InterPro:
CATH: Carbon-nitrogen hydrolase
SCOP: Carbamilase
N-carbamoyl-D-amino acid hydrolase in PDB entry 1uf7, assembly 1, front view.
N-carbamoyl-D-amino acid hydrolase in PDB entry 1uf7, assembly 1, side view.
N-carbamoyl-D-amino acid hydrolase in PDB entry 1uf7, assembly 1, top view.
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