› 5ov6

X-ray diffraction
1.87Å resolution

Bacillus megaterium porphobilinogen deaminase D82N mutant

Released:
DOI: 10.2210/pdb5ov6/pdb
PDB entry 5ov6 coloured by chain, front view.
PDB entry 5ov6 coloured by chain, side view.
PDB entry 5ov6 coloured by chain, top view.
Source organism: Priestia megaterium
Primary publication:
Structural studies of domain movement in active-site mutants of porphobilinogen deaminase from Bacillus megaterium.
Guo J, Erskine P, Coker AR, Wood SP, Cooper JB
Acta Crystallogr F Struct Biol Commun 73 612-620 (2017)
PMID: 29095155

Function and Biology Details

Reaction catalysed: 
4 porphobilinogen + H(2)O = hydroxymethylbilane + 4 NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184492 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Porphobilinogen deaminase Chain: A
Molecule details ›
Chain: A
Length: 310 amino acids
Theoretical weight: 34.29 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8GCA8 (Residues: 1-310; Coverage: 100%)
Gene names: C3744_10255, hemC
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand AWQ 1 x AWQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 48.99Å b: 62.69Å c: 91.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.21 0.253
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Human hydroxymethylbilane synthase: Molecular dynamics of the pyrrole chain elongation identifies step-specific residues that cause AIP.
Bung et al. (2018)
3 more

4 mentions without citation

Acute Intermittent Porphyria: An Overview of Therapy Developments and Future Perspectives Focusing on Stabilisation of HMBS and Proteostasis Regulators.
Bustad et al. (2021)
3 more