› 5hp5

X-ray diffraction
3.2Å resolution

Srtucture of human peptidylarginine deiminase type I (PAD1)

Released:
DOI: 10.2210/pdb5hp5/pdb
PDB entry 5hp5 coloured by chain, front view.
PDB entry 5hp5 coloured by chain, side view.
PDB entry 5hp5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Monomeric Form of Peptidylarginine Deiminase Type I Revealed by X-ray Crystallography and Small-Angle X-ray Scattering.
Saijo S, Nagai A, Kinjo S, Mashimo R, Akimoto M, Kizawa K, Yabe-Wada T, Shimizu N, Takahara H, Unno M
J Mol Biol 428 3058-73 (2016)
PMID: 27393304

Function and Biology Details

Reaction catalysed: 
Protein L-arginine + H(2)O = protein L-citrulline + NH(3)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193918 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-arginine deiminase type-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 684 amino acids
Theoretical weight: 77.29 KDa
Source organism: Homo sapiens
Expression system: unidentified plasmid
UniProt:
  • Canonical: Q9ULC6 (Residues: 1-663; Coverage: 100%)
Gene names: PAD1, PADI1, PDI1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 8 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P61
Unit cell:
a: 90.815Å b: 90.815Å c: 373.049Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.213 0.278
Expression system: unidentified plasmid

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Citations

13 review citations

Rheumatoid Arthritis-Associated Mechanisms of Porphyromonas gingivalis and Aggregatibacter actinomycetemcomitans.
Gómez-Bañuelos et al. (2019)
12 more

3 mentions without citation

Chemical biology of protein citrullination by the protein A arginine deiminases.
Mondal et al. (2021)
2 more