› 3b1u

X-ray diffraction
2.1Å resolution

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-193952 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-arginine deiminase type-4 Chain: A
Molecule details ›
Chain: A
Length: 671 amino acids
Theoretical weight: 74.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UM07 (Residues: 1-663; Coverage: 100%)
Gene names: PAD4, PADI4, PADI5, PDI5
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand YFF 1 x YFF
Ligand SO4 3 x SO4
Ligand CA 5 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: C2
Unit cell:
a: 146.422Å b: 60.468Å c: 115.506Å
α: 90° β: 124.43° γ: 90°
R-values:
R R work R free
0.221 0.219 0.25
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Protein Arginine Deiminases and Associated Citrullination: Physiological Functions and Diseases Associated with Dysregulation.
Witalison et al. (2015)
13 more

7 mentions without citation

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