› 1pv8

X-ray diffraction
2.2Å resolution

Crystal structure of a low activity F12L mutant of human porphobilinogen synthase

Released:
DOI: 10.2210/pdb1pv8/pdb
PDB entry 1pv8 coloured by chain, front view.
PDB entry 1pv8 coloured by chain, side view.
PDB entry 1pv8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase.
Breinig S, Kervinen J, Stith L, Wasson AS, Fairman R, Wlodawer A, Zdanov A, Jaffe EK
Nat Struct Biol 10 757-63 (2003)
PMID: 12897770

Function and Biology Details

Reaction catalysed: 
2 5-aminolevulinate = porphobilinogen + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146721 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Delta-aminolevulinic acid dehydratase Chains: A, B
Molecule details ›
Chains: A, B
Length: 330 amino acids
Theoretical weight: 36.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P13716 (Residues: 1-330; Coverage: 100%)
Gene name: ALAD
Sequence domains: Delta-aminolevulinic acid dehydratase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand PB1 1 x PB1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P63
Unit cell:
a: 89.571Å b: 89.571Å c: 153.19Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.199 0.284
Expression system: Escherichia coli

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Citations

13 review citations

Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases.
Poole LB. (2005)
12 more

18 mentions without citation

Allostery and the dynamic oligomerization of porphobilinogen synthase.
Jaffe et al. (2012)
17 more