› 3v77

X-ray diffraction
2.1Å resolution

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112446 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fumarylacetoacetase-like C-terminal domain-containing protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 224 amino acids
Theoretical weight: 24.14 KDa
Source organism: Oleispira antarctica
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: D2YW46 (Residues: 1-224; Coverage: 100%)
Sequence domains: Fumarylacetoacetate (FAA) hydrolase family
Structure domains: Fumarylacetoacetase-like, C-terminal domain

Ligands and Environments

3 bound ligands:
Ligand ZN 7 x ZN
Ligand TAR 9 x TAR
Ligand ACT 6 x ACT
1 modified residue:
Ligand MSE 18 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2221
Unit cell:
a: 158.265Å b: 161.386Å c: 114.836Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.199 0.256
Expression system: Escherichia coli BL21

Quick links

Citations

13 review citations

Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.
Santiago et al. (2016)
12 more

2 mentions without citation

Genome sequence and functional genomic analysis of the oil-degrading bacterium Oleispira antarctica.
Kube et al. (2013)
1 more