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Calcium in PDB 2sta: Anionic Salmon Trypsin in Complex with Squash Seed Inhibitor (Cucurbita Maxima Trypsin Inhibitor I)

Enzymatic activity of Anionic Salmon Trypsin in Complex with Squash Seed Inhibitor (Cucurbita Maxima Trypsin Inhibitor I)

All present enzymatic activity of Anionic Salmon Trypsin in Complex with Squash Seed Inhibitor (Cucurbita Maxima Trypsin Inhibitor I):
3.4.21.4;

Protein crystallography data

The structure of Anionic Salmon Trypsin in Complex with Squash Seed Inhibitor (Cucurbita Maxima Trypsin Inhibitor I), PDB code: 2sta was solved by R.Helland, G.I.Berglund, J.Otlewski, W.Apostoluk, O.A.Andersen, N.P.Willassen, A.O.Smalas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 62.300, 63.700, 82.300, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 23.3

Calcium Binding Sites:

The binding sites of Calcium atom in the Anionic Salmon Trypsin in Complex with Squash Seed Inhibitor (Cucurbita Maxima Trypsin Inhibitor I) (pdb code 2sta). 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 Anionic Salmon Trypsin in Complex with Squash Seed Inhibitor (Cucurbita Maxima Trypsin Inhibitor I), PDB code: 2sta:

Calcium binding site 1 out of 1 in 2sta

Go back to Calcium Binding Sites List in 2sta
Calcium binding site 1 out of 1 in the Anionic Salmon Trypsin in Complex with Squash Seed Inhibitor (Cucurbita Maxima Trypsin Inhibitor I)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Anionic Salmon Trypsin in Complex with Squash Seed Inhibitor (Cucurbita Maxima Trypsin Inhibitor I) within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca700

b:33.5
occ:1.00
 O E:VAL75 2.2 21.0 1.0
O E:ASN72 2.3 17.1 1.0
OE1 E:GLU70 2.5 16.4 1.0
O E:HOH755 2.5 21.5 1.0
OE2 E:GLU80 2.5 19.9 1.0
OE1 E:GLU77 2.7 27.2 1.0
CD E:GLU77 3.4 31.6 1.0
C E:VAL75 3.4 22.6 1.0
C E:ASN72 3.5 17.4 1.0
CD E:GLU70 3.5 18.2 1.0
CD E:GLU80 3.5 22.8 1.0
CG E:GLU77 3.7 27.2 1.0
CG E:GLU80 3.9 20.1 1.0
OE2 E:GLU70 3.9 18.7 1.0
CA E:ILE73 4.1 17.9 1.0
N E:VAL75 4.1 19.5 1.0
N E:GLU77 4.2 21.3 1.0
C E:ILE73 4.2 19.5 1.0
N E:ILE73 4.2 17.0 1.0
CA E:THR76 4.3 20.9 1.0
O E:HOH746 4.3 24.3 1.0
N E:THR76 4.3 21.7 1.0
CA E:VAL75 4.3 21.8 1.0
O E:ILE73 4.3 19.3 1.0
OE2 E:GLU77 4.4 30.8 1.0
N E:ASN72 4.4 14.8 1.0
CB E:GLU77 4.5 24.5 1.0
CA E:ASN72 4.5 15.6 1.0
OE1 E:GLU80 4.6 22.5 1.0
C E:THR76 4.6 22.3 1.0
N E:HIS71 4.7 15.8 1.0
CG E:GLU70 4.8 17.2 1.0
N E:LYS74 4.8 19.7 1.0
CB E:VAL75 4.8 22.1 1.0
CA E:GLU70 4.9 15.6 1.0
CB E:ASN72 4.9 15.9 1.0
CB E:GLU70 5.0 14.9 1.0

Reference:

R.Helland, G.I.Berglund, J.Otlewski, W.Apostoluk, O.A.Andersen, N.P.Willassen, A.O.Smalas. High-Resolution Structures of Three New Trypsin-Squash-Inhibitor Complexes: A Detailed Comparison with Other Trypsins and Their Complexes. Acta Crystallogr.,Sect.D V. 55 139 1999.
ISSN: ISSN 0907-4449
PubMed: 10089404
DOI: 10.1107/S090744499801052X
Page generated: Fri Jul 12 16:08:12 2024

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