› 3ppd

X-ray diffraction
1.5Å resolution

GGVLVN segment from Human Prostatic Acid Phosphatase Residues 260-265, involved in Semen-Derived Enhancer of Viral Infection

Released:
DOI: 10.2210/pdb3ppd/pdb
PDB entry 3ppd coloured by chain, front view.
PDB entry 3ppd coloured by chain, side view.
PDB entry 3ppd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation.
Sievers SA, Karanicolas J, Chang HW, Zhao A, Jiang L, Zirafi O, Stevens JT, Münch J, Baker D, Eisenberg D
Nature 475 96-100 (2011)
PMID: 21677644

Function and Biology Details

Reactions catalysed: 
A phosphate monoester + H(2)O = an alcohol + phosphate
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147311 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PAPf39 Chain: A
Molecule details ›
Chain: A
Length: 6 amino acids
Theoretical weight: 558 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P15309 (Residues: 260-265; Coverage: 2%)
Gene names: ACP3, ACPP

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand ACY 1 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 4.834Å b: 17.682Å c: 40.322Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.178 0.219
Expression system: Not provided

Quick links

Citations

61 review citations

The amyloid state of proteins in human diseases.
Eisenberg et al. (2012)
60 more

9 mentions without citation

New targets for HIV drug discovery.
Puhl et al. (2019)
8 more