› 3so3

X-ray diffraction
2.1Å resolution

Structures of Fab-Protease Complexes Reveal a Highly Specific Non-Canonical Mechanism of Inhibition.

Released:
DOI: 10.2210/pdb3so3/pdb
PDB entry 3so3 coloured by chain, front view.
PDB entry 3so3 coloured by chain, side view.
PDB entry 3so3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A reverse binding motif that contributes to specific protease inhibition by antibodies.
Schneider EL, Lee MS, Baharuddin A, Goetz DH, Farady CJ, Ward M, Wang CI, Craik CS
J Mol Biol 415 699-715 (2012)
PMID: 22154938

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:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-212879 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (4 distinct):
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
A11 FAB light chain Chain: B
Molecule details ›
Chain: B
Length: 217 amino acids
Theoretical weight: 23.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
Structure domains: Immunoglobulins
A11 FAB heavy chain Chain: C
Molecule details ›
Chain: C
Length: 228 amino acids
Theoretical weight: 23.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
Structure domains: Immunoglobulins

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, FRU
Carbohydrate polymer
1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P64
Unit cell:
a: 130.598Å b: 130.598Å c: 96.941Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.162 0.161 0.194
Expression systems:
  • Escherichia coli
  • Escherichia coli BL21

Quick links

Citations

4 review citations

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)
3 more

4 mentions without citation

A reverse binding motif that contributes to specific protease inhibition by antibodies.
Schneider et al. (2012)
3 more