› 2f9n

X-ray diffraction
1.6Å resolution

Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant K192Q/D216G in Complex with Leupeptin

Released:
DOI: 10.2210/pdb2f9n/pdb
PDB entry 2f9n coloured by chain, front view.
PDB entry 2f9n coloured by chain, side view.
PDB entry 2f9n coloured by chain, top view.
Source organisms:
Primary publication:
X-ray structures of free and leupeptin-complexed human alphaI-tryptase mutants: indication for an alpha-->beta-tryptase transition.
Rohr KB, Selwood T, Marquardt U, Huber R, Schechter NM, Bode W, Than ME
J Mol Biol 357 195-209 (2006)
PMID: 16414069

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-, but with more restricted specificity than trypsin.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162690 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Tryptase alpha/beta-1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 245 amino acids
Theoretical weight: 27.66 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q15661 (Residues: 31-275; Coverage: 95%)
Gene names: TPS1, TPS2, TPSAB1, TPSB1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Leupeptin Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 4 amino acids
Theoretical weight: 430 Da
Source organism: Streptomyces roseus
Expression system: Not provided

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
2 bound ligands:
Ligand BU3 4 x BU3
Ligand NAG 2 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P212121
Unit cell:
a: 83.31Å b: 88.57Å c: 163.37Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.236
Expression systems:
  • Spodoptera frugiperda
  • Not provided

Quick links

Citations

3 review citations

Serine proteases.
Di Cera E. (2009)
2 more

4 mentions without citation

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