› 4hgc

X-ray diffraction
1.29Å resolution

Crystal structure of bovine trypsin complexed with sfti-1 analog containing a peptoid residue at position p1

Released:
DOI: 10.2210/pdb4hgc/pdb
PDB entry 4hgc coloured by chain, front view.
PDB entry 4hgc coloured by chain, side view.
PDB entry 4hgc coloured by chain, top view.
Source organisms:
Primary publication:
Structure of a proteolytically resistant analogue of (NLys)5SFTI-1 in complex with trypsin: evidence for the direct participation of the Ser214 carbonyl group in serine protease-mediated proteolysis.
Krzywda S, Jaskolski M, Rolka K, Stawikowski MJ
Acta Crystallogr D Biol Crystallogr 70 668-75 (2014)
PMID: 24598736

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133355 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease 1 Chain: A
Molecule details ›
Chain: A
Length: 223 amino acids
Theoretical weight: 23.32 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00760 (Residues: 24-246; Coverage: 97%)
Gene names: PRSS1, TRP1, TRY1, TRYP1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Trypsin inhibitor 1 Chain: I
Molecule details ›
Chain: I
Length: 14 amino acids
Theoretical weight: 1.53 KDa
Source organism: Helianthus annuus
Expression system: Not provided
UniProt:
  • Canonical: Q4GWU5 (Residues: 40-53; Coverage: 45%)
Gene name: sfti1

Ligands and Environments

3 bound ligands:
Ligand CA 1 x CA
Ligand GOL 5 x GOL
Ligand SO4 3 x SO4
1 modified residue:
Ligand NLY 1 x NLY

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 60.12Å b: 64.14Å c: 70.04Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.127 0.126 0.157
Expression system: Not provided

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Citations

1 review citation

Amino acid modifications for conformationally constraining naturally occurring and engineered peptide backbones: Insights from the Protein Data Bank.
Di Costanzo et al. (2018)
4 other articles