› 6ftq

X-ray diffraction
2.08Å resolution

Crystal structure of human beta-ureidopropionase (beta-alanine synthase) - mutant T299C

Released:
DOI: 10.2210/pdb6ftq/pdb
PDB 6ftq coloured by chain and viewed from the front.
PDB 6ftq coloured by chain and viewed from the side.
PDB 6ftq coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Crystal structure and pH-dependent allosteric regulation of human ��-ureidopropionase, an enzyme involved in anticancer drug metabolism.
Maurer D, Lohkamp B, Krumpel M, Widersten M, Dobritzsch D
Biochem. J. 475 2395-2416 (2018)
PMID: 29976570

Function and Biology Details

Reaction catalysed: 
3-ureidopropanoate + H(2)O = beta-alanine + CO(2) + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-ureidopropionase Chain: A
Molecule details ›
Chain: A
Length: 390 amino acids
Theoretical weight: 43.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9UBR1 (Residues: 1-384; Coverage: 100%)
Gene names: BUP1, UPB1
Sequence domains: Carbon-nitrogen hydrolase

Ligands and Environments

No bound ligands
1 modified residue:
Ligand CSD 1 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: C2221
Unit cell:
a: 86.815Å b: 104.244Å c: 102.808Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.175 0.199
Expression system: Escherichia coli BL21

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Citations

1 citations in other articles

Cryo-EM and directed evolution reveal how Arabidopsis nitrilase specificity is influenced by its quaternary structure.
Mulelu et al. (2019)