› 3h50

X-ray diffraction
1.6Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185734 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cupin type-2 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 114 amino acids
Theoretical weight: 12.33 KDa
Source organism: Xanthomonas campestris pv. campestris
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8PBM3 (Residues: 1-113; Coverage: 100%)
Gene names: XCC1096, tcmJ
Sequence domains: Cupin domain
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand ACT 2 x ACT
1 modified residue:
Ligand MSE 2 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: C2
Unit cell:
a: 48.92Å b: 72.03Å c: 32.75Å
α: 90° β: 110.76° γ: 90°
R-values:
R R work R free
0.184 0.182 0.22
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

First- and second-shell metal binding residues in human proteins are disproportionately associated with disease-related SNPs.
Levy et al. (2011)
1 more

4 mentions without citation

Experimental phasing using zinc anomalous scattering.
Cha et al. (2012)
3 more