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Calcium in PDB 5xwa: Crystal Structure of Porcine Pancreatic Trypsin with Tripeptide Inhibitor, Pry, at pH 10

Enzymatic activity of Crystal Structure of Porcine Pancreatic Trypsin with Tripeptide Inhibitor, Pry, at pH 10

All present enzymatic activity of Crystal Structure of Porcine Pancreatic Trypsin with Tripeptide Inhibitor, Pry, at pH 10:
3.4.21.4;

Protein crystallography data

The structure of Crystal Structure of Porcine Pancreatic Trypsin with Tripeptide Inhibitor, Pry, at pH 10, PDB code: 5xwa was solved by N.S.Saikhedkar, A.S.Bhoite, A.P.Giri, K.A.Kulkarni, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.58 / 1.90
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 83.165, 83.165, 135.232, 90.00, 90.00, 120.00
R / Rfree (%) 15.3 / 18.2

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Porcine Pancreatic Trypsin with Tripeptide Inhibitor, Pry, at pH 10 (pdb code 5xwa). 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 Crystal Structure of Porcine Pancreatic Trypsin with Tripeptide Inhibitor, Pry, at pH 10, PDB code: 5xwa:

Calcium binding site 1 out of 1 in 5xwa

Go back to Calcium Binding Sites List in 5xwa
Calcium binding site 1 out of 1 in the Crystal Structure of Porcine Pancreatic Trypsin with Tripeptide Inhibitor, Pry, at pH 10


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Porcine Pancreatic Trypsin with Tripeptide Inhibitor, Pry, at pH 10 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca300

b:13.2
occ:1.00
 OE2 A:GLU70 2.3 14.0 1.0
OE1 A:GLU60 2.3 12.0 1.0
O A:ASN62 2.3 11.1 1.0
O A:HOH444 2.3 11.4 1.0
O A:VAL65 2.3 14.1 1.0
OE1 A:GLU67 2.4 17.6 1.0
CD A:GLU67 3.2 27.6 1.0
CD A:GLU70 3.3 12.9 1.0
CD A:GLU60 3.4 12.2 1.0
C A:VAL65 3.5 15.7 1.0
C A:ASN62 3.5 14.4 1.0
CG A:GLU67 3.7 28.4 1.0
CG A:GLU70 3.7 13.8 1.0
OE2 A:GLU60 3.8 13.0 1.0
N A:GLU67 4.1 15.7 1.0
CA A:LEU66 4.2 15.8 1.0
N A:VAL65 4.2 12.7 1.0
N A:LEU66 4.2 13.6 1.0
OE2 A:GLU67 4.2 20.7 1.0
CA A:ILE63 4.2 10.4 1.0
N A:ILE63 4.3 10.5 1.0
N A:ASN62 4.4 11.9 1.0
CA A:ASN62 4.4 10.9 1.0
O A:HOH443 4.4 21.0 1.0
CA A:VAL65 4.4 13.3 1.0
OE1 A:GLU70 4.5 14.6 1.0
C A:ILE63 4.5 11.1 1.0
CB A:GLU67 4.6 21.2 1.0
C A:LEU66 4.6 19.5 1.0
CG A:GLU60 4.7 9.3 1.0
CB A:ASN62 4.7 11.7 1.0
N A:HIS61 4.7 9.8 1.0
N A:ASP64 4.8 11.6 1.0
O A:HOH501 4.8 29.2 1.0
CA A:GLU60 4.9 11.8 1.0
CB A:GLU60 4.9 12.5 1.0
O A:ILE63 4.9 11.3 1.0

Reference:

N.S.Saikhedkar, R.S.Joshi, A.S.Bhoite, R.Mohandasan, A.K.Yadav, M.Fernandes, K.A.Kulkarni, A.P.Giri. Tripeptides Derived From Reactive Centre Loop of Potato Type II Protease Inhibitors Preferentially Inhibit Midgut Proteases of Helicoverpa Armigera. Insect Biochem. Mol. Biol. V. 95 17 2018.
ISSN: ISSN 1879-0240
PubMed: 29486250
DOI: 10.1016/J.IBMB.2018.02.001
Page generated: Mon Jul 15 15:11:02 2024

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