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Calcium in PDB 2tgd: Lack of the Transition State Stabilization Site Is A Factor in the Inactivity of Trypsinogen, A Serine Protease Zymogen. Structure of Dfp Inhibited Bovine Trypsinogen at 2.1 Angstroms Resolution

Protein crystallography data

The structure of Lack of the Transition State Stabilization Site Is A Factor in the Inactivity of Trypsinogen, A Serine Protease Zymogen. Structure of Dfp Inhibited Bovine Trypsinogen at 2.1 Angstroms Resolution, PDB code: 2tgd was solved by M.O.Jones, R.M.Stroud, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.10
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 55.150, 55.150, 109.300, 90.00, 90.00, 120.00
R / Rfree (%) 18.2 / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Lack of the Transition State Stabilization Site Is A Factor in the Inactivity of Trypsinogen, A Serine Protease Zymogen. Structure of Dfp Inhibited Bovine Trypsinogen at 2.1 Angstroms Resolution (pdb code 2tgd). 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 Lack of the Transition State Stabilization Site Is A Factor in the Inactivity of Trypsinogen, A Serine Protease Zymogen. Structure of Dfp Inhibited Bovine Trypsinogen at 2.1 Angstroms Resolution, PDB code: 2tgd:

Calcium binding site 1 out of 1 in 2tgd

Go back to Calcium Binding Sites List in 2tgd
Calcium binding site 1 out of 1 in the Lack of the Transition State Stabilization Site Is A Factor in the Inactivity of Trypsinogen, A Serine Protease Zymogen. Structure of Dfp Inhibited Bovine Trypsinogen at 2.1 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Lack of the Transition State Stabilization Site Is A Factor in the Inactivity of Trypsinogen, A Serine Protease Zymogen. Structure of Dfp Inhibited Bovine Trypsinogen at 2.1 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca247

b:8.0
occ:1.00
O A:VAL75 2.2 2.0 1.0
OE1 A:GLU70 2.4 2.0 1.0
OE2 A:GLU80 2.4 2.0 1.0
O A:ASN72 2.5 2.0 1.0
O A:HOH263 2.5 12.0 1.0
C A:VAL75 3.3 8.0 1.0
CD A:GLU70 3.4 3.0 1.0
C A:ASN72 3.4 2.0 1.0
CD A:GLU80 3.5 16.0 1.0
OE2 A:GLU77 3.6 18.0 1.0
CG A:GLU77 3.7 11.0 1.0
OE2 A:GLU70 3.9 4.0 1.0
CG A:GLU80 4.0 2.0 1.0
N A:VAL76 4.0 6.0 1.0
CA A:VAL76 4.0 7.0 1.0
CD A:GLU77 4.1 9.0 1.0
N A:VAL75 4.1 6.0 1.0
CA A:ILE73 4.1 8.0 1.0
N A:ILE73 4.2 2.0 1.0
N A:ASN72 4.2 13.0 1.0
N A:GLU77 4.3 2.0 1.0
CA A:VAL75 4.3 12.0 1.0
CA A:ASN72 4.4 10.0 1.0
C A:ILE73 4.4 12.0 1.0
N A:ASP71 4.5 9.0 1.0
O A:HOH249 4.5 14.0 1.0
CG A:GLU70 4.6 8.0 1.0
CB A:GLU70 4.6 3.0 1.0
CB A:ASN72 4.6 5.0 1.0
C A:VAL76 4.7 9.0 1.0
OE1 A:GLU80 4.7 2.0 1.0
CB A:GLU77 4.7 3.0 1.0
CA A:GLU70 4.7 2.0 1.0
N A:ASN74 4.8 2.0 1.0
O A:HOH287 4.9 11.0 1.0
CB A:VAL75 4.9 7.0 1.0
O A:ILE73 4.9 2.0 1.0
C A:ASP71 5.0 18.0 1.0

Reference:

M.O.Jones, R.M.Stroud. Lack of the Transition State Stabilization Site Is A Factor in the Inactivity of Trypsinogen, A Serine Protease Zymogen. Structure of Dfp Inhibited Bovine Trypsinogen at 2.1 Angstroms Resolution To Be Published.
Page generated: Fri Jul 12 17:43:30 2024

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