X-ray diffraction
1.85Å resolution

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


Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
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
  • 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:
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 R work R free
0.179 0.179 0.205
Expression system: Cricetulus griseus