› 3ncl

X-ray diffraction
1.19Å resolution

Crystal Structure of MT-SP1 bound to Benzamidine Phosphonate Inhibitor

Released:
DOI: 10.2210/pdb3ncl/pdb
PDB entry 3ncl coloured by chain, front view.
PDB entry 3ncl coloured by chain, side view.
PDB entry 3ncl coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Peptide length and leaving-group sterics influence potency of peptide phosphonate protease inhibitors.
Brown CM, Ray M, Eroy-Reveles AA, Egea P, Tajon C, Craik CS
Chem Biol 18 48-57 (2011)
PMID: 21276938

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: 26.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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

2 bound ligands:
Ligand CCZ 1 x CCZ
Ligand FMT 3 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2
Unit cell:
a: 74.915Å b: 80.24Å c: 40.539Å
α: 90° β: 95.82° γ: 90°
R-values:
R R work R free
0.134 0.133 0.156
Expression system: Escherichia coli

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Citations

1 review citation

Priming of SARS-CoV-2 S protein by several membrane-bound serine proteinases could explain enhanced viral infectivity and systemic COVID-19 infection.
Fuentes-Prior P. (2021)
7 other articles

2 mentions without citation

Peptide length and leaving-group sterics influence potency of peptide phosphonate protease inhibitors.
Brown et al. (2011)
1 more