› 1ym0

X-ray diffraction
2.06Å resolution

Crystal Structure of Earthworm Fibrinolytic Enzyme Component B: a Novel, Glycosylated Two-chained Trypsin

Released:
DOI: 10.2210/pdb1ym0/pdb
PDB entry 1ym0 coloured by chain, front view.
PDB entry 1ym0 coloured by chain, side view.
PDB entry 1ym0 coloured by chain, top view.
Source organism: Eisenia fetida
Primary publication:
Crystal structure of earthworm fibrinolytic enzyme component B: a novel, glycosylated two-chained trypsin.
Wang F, Wang C, Li M, Zhang JP, Gui LL, An XM, Chang WR
J Mol Biol 348 671-85 (2005)
PMID: 15826663

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Peptidase S1 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 238 amino acids
Theoretical weight: 25.33 KDa
Source organism: Eisenia fetida
UniProt:
  • Canonical: Q3HR18 (Residues: 8-245; Coverage: 97%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
fibrinotic enzyme component B Chain: B
Molecule details ›
Chain: B
Length: 27 amino acids
Theoretical weight: 2.82 KDa
Source organism: Eisenia fetida

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, MAN, FUC
Carbohydrate polymer
2 bound ligands:
Ligand MG 3 x MG
Ligand SO4 2 x SO4
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6B
Spacegroup: P6322
Unit cell:
a: 96.353Å b: 96.353Å c: 150.809Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.181 0.192

Quick links

Citations

4 review citations

Bioactive proteins and peptides isolated from Chinese medicines with pharmaceutical potential.
Wong et al. (2014)
3 more

2 mentions without citation

The expanding diversity of serine hydrolases.
Botos et al. (2007)
1 more