› 4n22

X-ray diffraction
1.89Å resolution

Crystal structure of Protein Arginine Deiminase 2 (50 uM Ca2+)

Released:
DOI: 10.2210/pdb4n22/pdb
PDB entry 4n22 coloured by chain, front view.
PDB entry 4n22 coloured by chain, side view.
PDB entry 4n22 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Protein arginine deiminase 2 binds calcium in an ordered fashion: implications for inhibitor design.
Slade DJ, Fang P, Dreyton CJ, Zhang Y, Fuhrmann J, Rempel D, Bax BD, Coonrod SA, Lewis HD, Guo M, Gross ML, Thompson PR
ACS Chem Biol 10 1043-53 (2015)
PMID: 25621824

Function and Biology Details

Reaction catalysed: 
Protein L-arginine + H(2)O = protein L-citrulline + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195140 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-arginine deiminase type-2 Chain: A
Molecule details ›
Chain: A
Length: 690 amino acids
Theoretical weight: 78.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y2J8 (Residues: 1-665; Coverage: 100%)
Gene names: KIAA0994, PAD2, PADI2, PDI2
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand ACT 3 x ACT
Ligand GOL 1 x GOL
Ligand CA 2 x CA
Ligand MPD 1 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: C2
Unit cell:
a: 201.823Å b: 51.642Å c: 75.756Å
α: 90° β: 105.54° γ: 90°
R-values:
R R work R free
0.172 0.17 0.208
Expression system: Escherichia coli

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Citations

24 review citations

Chemical biology of protein arginine modifications in epigenetic regulation.
Fuhrmann et al. (2015)
23 more

1 mention without citation

Protein arginine deiminase 2 binds calcium in an ordered fashion: implications for inhibitor design.
Slade et al. (2015)