› 1wda

X-ray diffraction
2.3Å resolution

Crystal structure of human peptidylarginine deiminase type4 (PAD4) in complex with benzoyl-L-arginine amide

Released:
DOI: 10.2210/pdb1wda/pdb
PDB entry 1wda coloured by chain, front view.
PDB entry 1wda coloured by chain, side view.
PDB entry 1wda coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for Ca(2+)-induced activation of human PAD4.
Arita K, Hashimoto H, Shimizu T, Nakashima K, Yamada M, Sato M
Nat Struct Mol Biol 11 777-83 (2004)
PMID: 15247907

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 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: 670 amino acids
Theoretical weight: 74.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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 CA 5 x CA
Ligand SO4 3 x SO4
Ligand BAG 1 x BAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: C2
Unit cell:
a: 146.133Å b: 60.045Å c: 115.406Å
α: 90° β: 124.23° γ: 90°
R-values:
R R work R free
0.215 0.21 0.252
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

58 review citations

Citrullination: a posttranslational modification in health and disease.
György et al. (2006)
57 more

25 mentions without citation

Peptidylarginine deiminases in citrullination, gene regulation, health and pathogenesis.
Wang et al. (2013)
24 more