› 4btx

X-ray diffraction
2.78Å resolution

Crystal structure of human vascular adhesion protein-1 in complex with pyridazinone inhibitors

Released:
DOI: 10.2210/pdb4btx/pdb
PDB entry 4btx coloured by chain, front view.
PDB entry 4btx coloured by chain, side view.
PDB entry 4btx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Novel pyridazinone inhibitors for vascular adhesion protein-1 (VAP-1): old target-new inhibition mode.
Bligt-Lindén E, Pihlavisto M, Szatmári I, Otwinowski Z, Smith DJ, Lázár L, Fülöp F, Salminen TA
J Med Chem 56 9837-48 (2013)
PMID: 24304424

Function and Biology Details

Reaction catalysed: 
RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172603 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Amine oxidase [copper-containing] 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 737 amino acids
Theoretical weight: 81.9 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: Q16853 (Residues: 27-763; Coverage: 97%)
Gene names: AOC3, VAP1
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer
5 bound ligands:
Ligand CU 2 x CU
Ligand CA 4 x CA
Ligand NAG 7 x NAG
Ligand WF8 2 x WF8
Ligand MAN 1 x MAN
1 modified residue:
Ligand TPQ 2 x TPQ

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P6522
Unit cell:
a: 226.35Å b: 226.35Å c: 217.226Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.181 0.237

Quick links

Citations

6 review citations

Vascular adhesion protein-1: Role in human pathology and application as a biomarker.
Pannecoeck et al. (2015)
5 more

4 mentions without citation

Human Copper-Containing Amine Oxidases in Drug Design and Development.
Vakal et al. (2020)
3 more