› 3edy

X-ray diffraction
1.85Å resolution

Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1

Released:
DOI: 10.2210/pdb3edy/pdb
PDB entry 3edy coloured by chain, front view.
PDB entry 3edy coloured by chain, side view.
PDB entry 3edy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
Guhaniyogi J, Sohar I, Das K, Stock AM, Lobel P
J Biol Chem 284 3985-97 (2009)
PMID: 19038967

Function and Biology Details

Reaction catalysed: 
Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127119 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tripeptidyl-peptidase 1 Chain: A
Molecule details ›
Chain: A
Length: 544 amino acids
Theoretical weight: 59.37 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: O14773 (Residues: 20-563; Coverage: 100%)
Gene names: CLN2, GIG1, TPP1, UNQ267/PRO304
Sequence domains:
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

3 bound ligands:
Ligand CA 1 x CA
Ligand NAG 4 x NAG
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P212121
Unit cell:
a: 59.807Å b: 93.173Å c: 102.479Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 0.205
Expression system: Cricetulus griseus

Quick links

Citations

6 review citations

Cell biology and function of neuronal ceroid lipofuscinosis-related proteins.
Kollmann et al. (2013)
5 more

10 mentions without citation

G-Quadruplex-Binding Proteins: Promising Targets for Drug Design.
Shu et al. (2022)
9 more