› 1ypn

X-ray diffraction
2.3Å resolution

REDUCED FORM HYDROXYMETHYLBILANE SYNTHASE (K59Q MUTANT) CRYSTAL STRUCTURE AFTER 2 HOURS IN A FLOW CELL DETERMINED BY TIME-RESOLVED LAUE DIFFRACTION

Released:
DOI: 10.2210/pdb1ypn/pdb
PDB entry 1ypn coloured by chain, front view.
PDB entry 1ypn coloured by chain, side view.
PDB entry 1ypn coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Time-Resolved Structures of Hydroxymethylbilane Synthase (Lys59Gln Mutant) as It Isloaded with Substrate in the Crystal Determined by Laue Diffraction
Helliwell JR, Nieh YP, Cassetta A, Habash J, Carr PD, Ursby T, Wulff M, Thompson AW, Niemann AC, Haedener A
J. Chem. Soc. Faraday Trans. 94 2615-2622 (1998)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139322 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Porphobilinogen deaminase Chain: A
Molecule details ›
Chain: A
Length: 313 amino acids
Theoretical weight: 33.89 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P06983 (Residues: 1-313; Coverage: 100%)
Gene names: JW5932, b3805, hemC, popE
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand DPM 1 x DPM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID09
Spacegroup: P21212
Unit cell:
a: 88.47Å b: 76.15Å c: 50.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.29
Expression system: Escherichia coli

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