› 1oc1

X-ray diffraction
2.2Å resolution

ISOPENICILLIN N SYNTHASE aminoadipoyl-cysteinyl-aminobutyrate-FE COMPLEX

Released:
DOI: 10.2210/pdb1oc1/pdb
PDB entry 1oc1 coloured by chain, front view.
PDB entry 1oc1 coloured by chain, side view.
PDB entry 1oc1 coloured by chain, top view.
Source organism: Aspergillus nidulans FGSC A4
Primary publication:
Structural studies on the reaction of isopenicillin N synthase with the substrate analogue delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-alpha-aminobutyrate.
Long AJ, Clifton IJ, Roach PL, Baldwin JE, Schofield CJ, Rutledge PJ
Biochem J 372 687-93 (2003)
PMID: 12622704

Function and Biology Details

Reaction catalysed: 
N-((5S)-5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + O(2) = isopenicillin N + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138628 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isopenicillin N synthase Chain: A
Molecule details ›
Chain: A
Length: 331 amino acids
Theoretical weight: 37.56 KDa
Source organism: Aspergillus nidulans FGSC A4
Expression system: Escherichia coli
UniProt:
  • Canonical: P05326 (Residues: 1-331; Coverage: 100%)
Gene names: AN2622, ipnA, ips
Sequence domains:
Structure domains: B-lactam Antibiotic, Isopenicillin N Synthase; Chain

Ligands and Environments

3 bound ligands:
Ligand ASV 1 x ASV
Ligand FE2 1 x FE2
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 100.976Å b: 100.976Å c: 115.658Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.173 0.197
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins.
Clifton et al. (2006)
3 more

1 mention without citation

Anaerobic fixed-target serial crystallography.
Rabe et al. (2020)