› 1klt

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF PMSF-TREATED HUMAN CHYMASE AT 1.9 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1klt/pdb
PDB entry 1klt coloured by chain, front view.
PDB entry 1klt coloured by chain, side view.
PDB entry 1klt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of phenylmethanesulfonyl fluoride-treated human chymase at 1.9 A.
McGrath ME, Mirzadegan T, Schmidt BF
Biochemistry 36 14318-24 (1997)
PMID: 9400368

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150125 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chymase Chain: A
Molecule details ›
Chain: A
Length: 226 amino acids
Theoretical weight: 25.05 KDa
Source organism: Homo sapiens
Expression system: Bacillus subtilis
UniProt:
  • Canonical: P23946 (Residues: 22-247; Coverage: 99%)
Gene names: CMA1, CYH, CYM
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand PMS 1 x PMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 43.93Å b: 58.16Å c: 86.09Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.255
Expression system: Bacillus subtilis

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Citations

1 review citation

Structural and energetic determinants of the S1-site specificity in serine proteases.
Czapinska et al. (1999)
22 other articles

7 mentions without citation

Bioengineering a unique deimmunized bispecific targeted toxin that simultaneously recognizes human CD22 and CD19 receptors in a mouse model of B-cell metastases.
Vallera et al. (2010)
6 more