› 3ee6

X-ray diffraction
2.35Å resolution

Crystal Structure Analysis of Tripeptidyl peptidase -I

Released:
DOI: 10.2210/pdb3ee6/pdb
PDB entry 3ee6 coloured by chain, front view.
PDB entry 3ee6 coloured by chain, side view.
PDB entry 3ee6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
Pal A, Kraetzner R, Gruene T, Grapp M, Schreiber K, Grønborg M, Urlaub H, Becker S, Asif AR, Gärtner J, Sheldrick GM, Steinfeld R
J Biol Chem 284 3976-84 (2009)
PMID: 19038966

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:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-127120 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tripeptidyl-peptidase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 571 amino acids
Theoretical weight: 62.38 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: O14773 (Residues: 1-563; Coverage: 100%)
Gene names: CLN2, GIG1, TPP1, UNQ267/PRO304
Sequence domains:
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

5 bound ligands:
Ligand NAG 8 x NAG
Ligand ZN 8 x ZN
Ligand CL 2 x CL
Ligand CA 2 x CA
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21212
Unit cell:
a: 113.45Å b: 128.93Å c: 100.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.218 0.262
Expression system: Homo sapiens

Quick links

Citations

4 review citations

New families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases.
Oda K. (2012)
3 more

5 mentions without citation

Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases.
Goettig P. (2016)
4 more