› 3cjp

X-ray diffraction
1.85Å resolution

Crystal structure of an uncharacterized amidohydrolase CAC3332 from Clostridium acetobutylicum

Released:
DOI: 10.2210/pdb3cjp/pdb
PDB entry 3cjp coloured by chain, front view.
PDB entry 3cjp coloured by chain, side view.
PDB entry 3cjp coloured by chain, top view.
Source organism: Clostridium acetobutylicum ATCC 824
Entry authors: Malashkevich VN, Toro R, Ramagopal UA, Bonanno JB, Meyer A, Sauder JM, Burley SK, Almo SC, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188894 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amidohydrolase-related domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 272 amino acids
Theoretical weight: 30.31 KDa
Source organism: Clostridium acetobutylicum ATCC 824
Expression system: Escherichia coli
UniProt:
  • Canonical: Q97DY3 (Residues: 2-262; Coverage: 100%)
Gene name: CA_C3337
Sequence domains: Amidohydrolase
Structure domains: Metal-dependent hydrolases

Ligands and Environments

1 bound ligand:
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 47.628Å b: 77.273Å c: 72.661Å
α: 90° β: 96.09° γ: 90°
R-values:
R R work R free
0.187 0.184 0.241
Expression system: Escherichia coli

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