› 1vc3

X-ray diffraction
1.5Å resolution

Crystal Structure of L-Aspartate-alpha-Decarboxylase

Released:
DOI: 10.2210/pdb1vc3/pdb
PDB entry 1vc3 coloured by chain, front view.
PDB entry 1vc3 coloured by chain, side view.
PDB entry 1vc3 coloured by chain, top view.
Source organism: Thermus thermophilus
Entry authors: Nakajima O, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed: 
L-aspartate = beta-alanine + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero tetramer (preferred)
hetero octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-178099 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aspartate 1-decarboxylase beta chain Chain: A
Molecule details ›
Chain: A
Length: 24 amino acids
Theoretical weight: 2.82 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SKN7 (Residues: 1-24; Coverage: 20%)
Gene names: TTHA0606, panD
Aspartate 1-decarboxylase alpha chain Chain: B
Molecule details ›
Chain: B
Length: 96 amino acids
Theoretical weight: 10.3 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SKN7 (Residues: 26-120; Coverage: 79%)
Gene names: TTHA0606, panD
Sequence domains: Aspartate decarboxylase
Structure domains: Barwin-like endoglucanases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: I4
Unit cell:
a: 67.53Å b: 67.53Å c: 47.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.215 0.247
Expression system: Escherichia coli BL21(DE3)

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