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Calcium in PDB 1f2s: Crystal Structure of the Complex Formed Between Bovine Beta-Trypsin and Mcti-A, A Trypsin Inhibitor of Squash Family at 1.8 A Resolution

Enzymatic activity of Crystal Structure of the Complex Formed Between Bovine Beta-Trypsin and Mcti-A, A Trypsin Inhibitor of Squash Family at 1.8 A Resolution

All present enzymatic activity of Crystal Structure of the Complex Formed Between Bovine Beta-Trypsin and Mcti-A, A Trypsin Inhibitor of Squash Family at 1.8 A Resolution:
3.4.21.4;

Protein crystallography data

The structure of Crystal Structure of the Complex Formed Between Bovine Beta-Trypsin and Mcti-A, A Trypsin Inhibitor of Squash Family at 1.8 A Resolution, PDB code: 1f2s was solved by Y.Zhu, Q.Huang, M.Qian, Y.Jia, Y.Tang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 1.79
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 59.760, 55.550, 74.470, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 22.6

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Complex Formed Between Bovine Beta-Trypsin and Mcti-A, A Trypsin Inhibitor of Squash Family at 1.8 A Resolution (pdb code 1f2s). 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 the Complex Formed Between Bovine Beta-Trypsin and Mcti-A, A Trypsin Inhibitor of Squash Family at 1.8 A Resolution, PDB code: 1f2s:

Calcium binding site 1 out of 1 in 1f2s

Go back to Calcium Binding Sites List in 1f2s
Calcium binding site 1 out of 1 in the Crystal Structure of the Complex Formed Between Bovine Beta-Trypsin and Mcti-A, A Trypsin Inhibitor of Squash Family at 1.8 A Resolution


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 the Complex Formed Between Bovine Beta-Trypsin and Mcti-A, A Trypsin Inhibitor of Squash Family at 1.8 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca800

b:29.9
occ:1.00
 O E:VAL75 2.0 36.5 1.0
O E:ASN72 2.1 18.8 1.0
O E:HOH559 2.1 26.3 1.0
O E:HOH410 2.1 20.5 1.0
OE1 E:GLU70 2.4 27.7 1.0
OE2 E:GLU80 2.5 25.2 1.0
C E:VAL75 3.2 35.4 1.0
C E:ASN72 3.3 18.7 1.0
CD E:GLU70 3.5 26.8 1.0
CD E:GLU80 3.5 25.4 1.0
CG E:GLU80 3.9 25.2 1.0
OE2 E:GLU70 3.9 26.4 1.0
CA E:ILE73 4.0 24.2 1.0
N E:VAL76 4.1 36.5 1.0
CA E:VAL76 4.1 36.8 1.0
N E:ILE73 4.1 20.2 1.0
C E:ILE73 4.2 26.0 1.0
N E:VAL75 4.2 33.7 1.0
CA E:VAL75 4.3 33.9 1.0
N E:GLU77 4.3 35.3 1.0
CG E:GLU77 4.3 37.5 1.0
CA E:ASN72 4.3 20.0 1.0
O E:HOH453 4.4 30.3 1.0
N E:ASN72 4.4 19.7 1.0
OE2 E:GLU77 4.4 38.6 1.0
O E:ILE73 4.4 27.4 1.0
C E:VAL76 4.6 36.1 1.0
OE1 E:GLU80 4.6 27.0 1.0
CB E:ASN72 4.6 20.8 1.0
O E:HOH604 4.6 55.4 1.0
N E:ASN74 4.7 28.5 1.0
CG E:GLU70 4.7 25.5 1.0
N E:ASP71 4.7 20.7 1.0
CD E:GLU77 4.8 39.1 1.0
C E:ASN74 4.9 32.9 1.0
CB E:GLU70 5.0 22.5 1.0
CB E:GLU77 5.0 36.2 1.0
O E:HOH416 5.0 25.2 1.0

Reference:

Y.Zhu, Q.Huang, M.Qian, Y.Jia, Y.Tang. Crystal Structure of the Complex Formed Between Bovine Beta-Trypsin and Mcti-A, A Trypsin Inhibitor of Squash Family, at 1.8-A Resolution. J.Protein Chem. V. 18 505 1999.
ISSN: ISSN 0277-8033
PubMed: 10524768
DOI: 10.1023/A:1020690931043
Page generated: Mon Jul 7 14:45:35 2025

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