› 3p8g

X-ray diffraction
1.2Å resolution

Crystal Structure of MT-SP1 in complex with benzamidine

Released:
DOI: 10.2210/pdb3p8g/pdb
PDB entry 3p8g coloured by chain, front view.
PDB entry 3p8g coloured by chain, side view.
PDB entry 3p8g coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of catalytic domain of Matriptase in complex with Sunflower trypsin inhibitor-1.
Yuan C, Chen L, Meehan EJ, Daly N, Craik DJ, Huang M, Ngo JC
BMC Struct Biol 11 30 (2011)
PMID: 21693064

Function and Biology Details

Reaction catalysed: 
Cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195299 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Suppressor of tumorigenicity 14 protein Chain: A
Molecule details ›
Chain: A
Length: 241 amino acids
Theoretical weight: 26.48 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: Q9Y5Y6 (Residues: 615-855; Coverage: 28%)
Gene names: PRSS14, SNC19, ST14, TADG15
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

4 bound ligands:
Ligand SO4 3 x SO4
Ligand EDO 4 x EDO
Ligand BEN 1 x BEN
Ligand GSH 1 x GSH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C222
Unit cell:
a: 66.888Å b: 141.701Å c: 51.995Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 0.143 0.177
Expression system: Saccharomyces cerevisiae

Quick links

Citations

4 review citations

Iron refractory iron deficiency anemia.
De Falco et al. (2013)
3 more

3 mentions without citation

Cleavage specificity analysis of six type II transmembrane serine proteases (TTSPs) using PICS with proteome-derived peptide libraries.
Barré et al. (2014)
2 more