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Calcium in PDB 4wwy: Human Cationic Trypsin G193R Mutant in Complex with Bovine Pancreatic Trypsin Inhibitor

Enzymatic activity of Human Cationic Trypsin G193R Mutant in Complex with Bovine Pancreatic Trypsin Inhibitor

All present enzymatic activity of Human Cationic Trypsin G193R Mutant in Complex with Bovine Pancreatic Trypsin Inhibitor:
3.4.21.4;

Protein crystallography data

The structure of Human Cationic Trypsin G193R Mutant in Complex with Bovine Pancreatic Trypsin Inhibitor, PDB code: 4wwy was solved by A.Alloy, O.Kayode, A.S.Soares, R.Wang, E.S.Radisky, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.29 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 52.952, 63.227, 90.535, 90.00, 94.74, 90.00
R / Rfree (%) 17.1 / 20.7

Calcium Binding Sites:

The binding sites of Calcium atom in the Human Cationic Trypsin G193R Mutant in Complex with Bovine Pancreatic Trypsin Inhibitor (pdb code 4wwy). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Human Cationic Trypsin G193R Mutant in Complex with Bovine Pancreatic Trypsin Inhibitor, PDB code: 4wwy:

Calcium binding site 1 out of 1 in 4wwy

Go back to Calcium Binding Sites List in 4wwy
Calcium binding site 1 out of 1 in the Human Cationic Trypsin G193R Mutant in Complex with Bovine Pancreatic Trypsin Inhibitor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Human Cationic Trypsin G193R Mutant in Complex with Bovine Pancreatic Trypsin Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca301

b:48.8
occ:1.00
OE2 B:GLU70 2.6 16.7 1.0
NH1 B:ARG66 2.9 17.4 1.0
O B:ILE73 3.0 24.6 1.0
O B:HOH533 3.1 30.1 1.0
CE1 B:HIS40 3.5 19.0 1.0
NE2 B:HIS40 3.5 19.3 1.0
CD B:ARG66 3.7 15.2 1.0
CD B:GLU70 3.7 17.8 1.0
C B:ILE73 3.8 25.3 1.0
CA B:ILE73 3.9 23.3 1.0
CZ B:ARG66 4.0 17.0 1.0
CG B:GLU70 4.1 17.9 1.0
CZ B:PHE82 4.1 19.2 1.0
CB B:ILE73 4.2 23.9 1.0
NE B:ARG66 4.3 15.4 1.0
CE1 B:PHE82 4.4 18.2 1.0
CG2 B:ILE73 4.7 25.5 1.0
ND1 B:HIS40 4.8 17.9 1.0
OE1 B:GLU70 4.8 21.9 1.0
CD2 B:HIS40 4.9 20.1 1.0
CG B:ARG66 4.9 15.6 1.0
O B:ASN72 4.9 26.1 1.0
N B:GLU74 5.0 28.5 1.0

Reference:

A.P.Alloy, O.Kayode, R.Wang, A.Hockla, A.S.Soares, E.S.Radisky. Mesotrypsin Has Evolved Four Unique Residues to Cleave Trypsin Inhibitors As Substrates. J.Biol.Chem. V. 290 21523 2015.
ISSN: ESSN 1083-351X
PubMed: 26175157
DOI: 10.1074/JBC.M115.662429
Page generated: Sun Jul 14 14:24:47 2024

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