› 3bg4

X-ray diffraction
2.5Å resolution

The crystal structure of guamerin in complex with chymotrypsin and the development of an elastase-specific inhibitor

Released:
DOI: 10.2210/pdb3bg4/pdb
PDB entry 3bg4 coloured by chain, front view.
PDB entry 3bg4 coloured by chain, side view.
PDB entry 3bg4 coloured by chain, top view.
Source organisms:
Primary publication:
The crystal structure of guamerin in complex with chymotrypsin and the development of an elastase-specific inhibitor.
Kim H, Chu TT, Kim DY, Kim DR, Nguyen CM, Choi J, Lee JR, Hahn MJ, Kim KK
J Mol Biol 376 184-92 (2008)
PMID: 18155725

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-133426 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Chymotrypsin B chain A Chain: A
Molecule details ›
Chain: A
Length: 13 amino acids
Theoretical weight: 1.25 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00767 (Residues: 1-13; Coverage: 5%)
Chymotrypsin A chain B Chain: B
Molecule details ›
Chain: B
Length: 131 amino acids
Theoretical weight: 13.93 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 16-146; Coverage: 54%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Chymotrypsin A chain C Chain: C
Molecule details ›
Chain: C
Length: 97 amino acids
Theoretical weight: 10.07 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 149-245; Coverage: 40%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Guamerin Chain: D
Molecule details ›
Chain: D
Length: 57 amino acids
Theoretical weight: 6.13 KDa
Source organism: Hirudo nipponia
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P46443 (Residues: 1-57; Coverage: 100%)
Sequence domains: Antistasin family
Structure domains: Antistasin; domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 44.274Å b: 43.992Å c: 122.57Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.241
Expression system: Komagataella pastoris

Quick links

Citations

1 review citation

European Medicinal Leeches-New Roles in Modern Medicine.
Lemke et al. (2020)
6 other articles

2 mentions without citation

Peptide Backbone Composition and Protease Susceptibility: Impact of Modification Type, Position, and Tandem Substitution.
Werner et al. (2016)
1 more