› 3n5f

X-ray diffraction
2.75Å resolution

Crystal Structure of L-N-carbamoylase from Geobacillus stearothermophilus CECT43

Released:
DOI: 10.2210/pdb3n5f/pdb
PDB entry 3n5f coloured by chain, front view.
PDB entry 3n5f coloured by chain, side view.
PDB entry 3n5f coloured by chain, top view.
Source organism: Geobacillus stearothermophilus
Primary publication:
Mutational and structural analysis of L-N-carbamoylase reveals new insights into a peptidase M20/M25/M40 family member.
Martínez-Rodríguez S, García-Pino A, Las Heras-Vázquez FJ, Clemente-Jiménez JM, Rodríguez-Vico F, García-Ruiz JM, Loris R, Gavira JA
J Bacteriol 194 5759-68 (2012)
PMID: 22904279

Function and Biology Details

Reaction catalysed: 
N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H(2)O = L-2-amino acid + NH(3) + CO(2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176053 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-carbamoyl-L-amino acid hydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 408 amino acids
Theoretical weight: 44.17 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q53389 (Residues: 1-408; Coverage: 100%)
Gene name: amaB
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand IPA 2 x IPA
Ligand CO 2 x CO
Ligand CAC 1 x CAC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P21212
Unit cell:
a: 103.208Å b: 211.683Å c: 43.091Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.193 0.276
Expression system: Escherichia coli BL21(DE3)

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Citations

4 citation in other articles

Identification of differentially expressed proteins from Leishmania amazonensis associated with the loss of virulence of the parasites.
Magalhães et al. (2014)
3 more

2 mentions without citation

Mutational and structural analysis of L-N-carbamoylase reveals new insights into a peptidase M20/M25/M40 family member.
Martínez-Rodríguez et al. (2012)
1 more