1va0

X-ray diffraction
1.97Å resolution

Crystal Structure of the Native Form of Uroporphyrin III C-methyl transferase from Thermus thermophilus

Released:
Source organism: Thermus thermophilus HB8
Primary publication:
Structure of a closed-form uroporphyrinogen-III C-methyltransferase from Thermus thermophilus.
Acta Crystallogr D Biol Crystallogr 61 913-9 (2005)
PMID: 15983414

Function and Biology Details

Reaction catalysed:
(1a) S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-178088 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
uroporphyrinogen-III C-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 239 amino acids
Theoretical weight: 26.14 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SKH6 (Residues: 2-240; Coverage: 100%)
Gene name: TTHA0667
Sequence domains: Tetrapyrrole (Corrin/Porphyrin) Methylases
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 60.5Å b: 63.568Å c: 131.902Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.227
Expression system: Escherichia coli BL21(DE3)