› 1f2d

X-ray diffraction
2Å resolution

1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE

Released:
DOI: 10.2210/pdb1f2d/pdb
PDB entry 1f2d coloured by chain, front view.
PDB entry 1f2d coloured by chain, side view.
PDB entry 1f2d coloured by chain, top view.
Source organism: Cyberlindnera saturnus
Primary publication:
Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus.
Yao M, Ose T, Sugimoto H, Horiuchi A, Nakagawa A, Wakatsuki S, Yokoi D, Murakami T, Honma M, Tanaka I
J Biol Chem 275 34557-65 (2000)
PMID: 10938279

Function and Biology Details

Reaction catalysed: 
(1a) 1-aminocyclopropane-1-carboxylate = 2-aminobut-2-enoate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181704 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1-aminocyclopropane-1-carboxylate deaminase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 341 amino acids
Theoretical weight: 37.09 KDa
Source organism: Cyberlindnera saturnus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7M523 (Residues: 2-341; Coverage: 100%)
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand PLP 4 x PLP
1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: C2221
Unit cell:
a: 66.38Å b: 269.37Å c: 186.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.221 0.268
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Physiological implications of hydrogen sulfide: a whiff exploration that blossomed.
Wang R. (2012)
4 more

4 mentions without citation

Template-based structure modeling of protein-protein interactions.
Szilagyi et al. (2014)
3 more