Calcium in PDB 3tgk: Trypsinogen Mutant D194N and Deletion of Ile 16-Val 17 Complexed with Bovine Pancreatic Trypsin Inhibitor (Bpti)

Enzymatic activity of Trypsinogen Mutant D194N and Deletion of Ile 16-Val 17 Complexed with Bovine Pancreatic Trypsin Inhibitor (Bpti)

All present enzymatic activity of Trypsinogen Mutant D194N and Deletion of Ile 16-Val 17 Complexed with Bovine Pancreatic Trypsin Inhibitor (Bpti):
3.4.21.4;

Protein crystallography data

The structure of Trypsinogen Mutant D194N and Deletion of Ile 16-Val 17 Complexed with Bovine Pancreatic Trypsin Inhibitor (Bpti), PDB code: 3tgk was solved by A.Pasternak, A.White, C.J.Jeffery, N.Medina, M.Cahoon, D.Ringe, L.Hedstrom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.70
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 92.580, 92.580, 62.030, 90.00, 90.00, 120.00
R / Rfree (%) 18.4 / 21.8

Calcium Binding Sites:

The binding sites of Calcium atom in the Trypsinogen Mutant D194N and Deletion of Ile 16-Val 17 Complexed with Bovine Pancreatic Trypsin Inhibitor (Bpti) (pdb code 3tgk). 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 Trypsinogen Mutant D194N and Deletion of Ile 16-Val 17 Complexed with Bovine Pancreatic Trypsin Inhibitor (Bpti), PDB code: 3tgk:

Calcium binding site 1 out of 1 in 3tgk

Go back to Calcium Binding Sites List in 3tgk
Calcium binding site 1 out of 1 in the Trypsinogen Mutant D194N and Deletion of Ile 16-Val 17 Complexed with Bovine Pancreatic Trypsin Inhibitor (Bpti)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Trypsinogen Mutant D194N and Deletion of Ile 16-Val 17 Complexed with Bovine Pancreatic Trypsin Inhibitor (Bpti) within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca500

b:10.9
occ:1.00
 OE2 E:GLU80 2.3 9.4 1.0
O E:VAL75 2.3 11.1 1.0
OE1 E:GLU70 2.3 9.4 1.0
O E:ASN72 2.4 9.7 1.0
OE1 E:GLU77 2.4 15.1 1.0
O E:HOH513 2.5 10.9 1.0
CD E:GLU77 3.3 16.2 1.0
CD E:GLU80 3.4 8.5 1.0
CD E:GLU70 3.4 10.1 1.0
C E:ASN72 3.5 9.1 1.0
C E:VAL75 3.5 11.7 1.0
CG E:GLU77 3.7 14.6 1.0
CG E:GLU80 3.8 11.3 1.0
OE2 E:GLU70 3.8 10.4 1.0
N E:GLU77 4.0 15.4 1.0
CA E:ILE73 4.2 9.1 1.0
OE2 E:GLU77 4.3 18.0 1.0
N E:ILE73 4.3 9.7 1.0
CB E:GLU77 4.3 17.1 1.0
N E:VAL75 4.3 10.7 1.0
N E:ASN72 4.3 8.9 1.0
CA E:LEU76 4.3 11.4 1.0
N E:LEU76 4.4 8.9 1.0
O E:HOH571 4.4 26.4 1.0
CA E:ASN72 4.5 8.9 1.0
OE1 E:GLU80 4.5 10.8 1.0
CA E:VAL75 4.5 11.5 1.0
C E:ILE73 4.5 8.8 1.0
C E:LEU76 4.6 13.9 1.0
N E:HIS71 4.6 10.3 1.0
CG E:GLU70 4.6 6.8 1.0
O E:HOH587 4.7 29.9 1.0
CB E:ASN72 4.8 9.0 1.0
CA E:GLU77 4.8 17.2 1.0
CA E:GLU70 4.8 9.2 1.0
CB E:GLU70 4.9 8.8 1.0
O E:ILE73 4.9 9.3 1.0
N E:ASN74 4.9 9.5 1.0

Reference:

A.Pasternak, A.White, C.J.Jeffery, N.Medina, M.Cahoon, D.Ringe, L.Hedstrom. The Energetic Cost of Induced Fit Catalysis: Crystal Structures of Trypsinogen Mutants with Enhanced Activity and Inhibitor Affinity. Protein Sci. V. 10 1331 2001.
ISSN: ISSN 0961-8368
PubMed: 11420435
DOI: 10.1110/PS.44101
Page generated: Sat Dec 12 04:31:31 2020

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