5vrc

X-ray diffraction
2Å resolution

Crystal structure for Methylobacterium extorquens PqqC (truncation of natural CD fusion)

Released:

Function and Biology Details

Reaction catalysed:
6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate + 3 O(2) = 4,5-dioxo-4,5-dihydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + 2 H(2)O(2) + 2 H(2)O 
Biochemical function:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional coenzyme PQQ synthesis protein C/D Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 280 amino acids
Theoretical weight: 31.84 KDa
Source organism: Methylorubrum extorquens AM1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q49150 (Residues: 1-260; Coverage: 70%)
Gene names: MexAM1_META1p1749, pqqCD
Sequence domains: TENA/THI-4/PQQC family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P212121
Unit cell:
a: 62.501Å b: 114.185Å c: 145.403Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.236
Expression system: Escherichia coli