› 7cnp

X-ray diffraction
1.6Å resolution

Crystal structure of Agrobacterium tumefaciens aconitase X (apo-form)

Released:
DOI: 10.2210/pdb7cnp/pdb
Model geometry
Fit model/data
PDB entry 7cnp coloured by chain, front view.
PDB entry 7cnp coloured by chain, side view.
PDB entry 7cnp coloured by chain, top view.
Source organism: Agrobacterium tumefaciens
Primary publication:
Crystal structures of aconitase X enzymes from bacteria and archaea provide insights into the molecular evolution of the aconitase superfamily.
Watanabe S, Murase Y, Watanabe Y, Sakurai Y, Tajima K
OpenAccess logo Commun Biol 4 687 (2021)
PMID: 34099860

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-242640 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cis-3-hydroxy-L-proline dehydratase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 579 amino acids
Theoretical weight: 60.64 KDa
Source organism: Agrobacterium tumefaciens
Expression system: Escherichia coli

Ligands and Environments

2 bound ligands:
Ligand FES 3 x FES
Ligand MG 3 x MG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P21
Unit cell:
a: 73.131Å b: 73.15Å c: 133.603Å
α: 90° β: 101.39° γ: 90°
R-values:
R R work R free
0.177 0.176 0.205
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The catalytic and structural basis of archaeal glycerophospholipid biosynthesis.
de Kok et al. (2022)
3 other articles

2 mentions without citation

Crystal structures of aconitase X enzymes from bacteria and archaea provide insights into the molecular evolution of the aconitase superfamily.
Watanabe et al. (2021)
1 more