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Calcium in PDB 1fy8: Crystal Structure of the DELTAILE16VAL17 Rat Anionic Trypsinogen-Bpti Complex

Enzymatic activity of Crystal Structure of the DELTAILE16VAL17 Rat Anionic Trypsinogen-Bpti Complex

All present enzymatic activity of Crystal Structure of the DELTAILE16VAL17 Rat Anionic Trypsinogen-Bpti Complex:
3.4.21.4;

Protein crystallography data

The structure of Crystal Structure of the DELTAILE16VAL17 Rat Anionic Trypsinogen-Bpti Complex, PDB code: 1fy8 was solved by A.Pasternak, A.White, C.J.Jeffery, 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 (°) 92.600, 92.600, 62.060, 90.00, 90.00, 120.00
R / Rfree (%) 18.3 / 21.4

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the DELTAILE16VAL17 Rat Anionic Trypsinogen-Bpti Complex (pdb code 1fy8). 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 DELTAILE16VAL17 Rat Anionic Trypsinogen-Bpti Complex, PDB code: 1fy8:

Calcium binding site 1 out of 1 in 1fy8

Go back to Calcium Binding Sites List in 1fy8
Calcium binding site 1 out of 1 in the Crystal Structure of the DELTAILE16VAL17 Rat Anionic Trypsinogen-Bpti Complex


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 DELTAILE16VAL17 Rat Anionic Trypsinogen-Bpti Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca500

b:11.7
occ:1.00
OE2 E:GLU80 2.3 12.0 1.0
OE1 E:GLU70 2.3 10.6 1.0
O E:VAL75 2.3 12.9 1.0
O E:ASN72 2.4 9.9 1.0
O E:HOH524 2.5 14.1 1.0
OE1 E:GLU77 2.6 16.2 1.0
CD E:GLU80 3.3 11.6 1.0
CD E:GLU70 3.4 12.1 1.0
CD E:GLU77 3.4 17.2 1.0
C E:ASN72 3.5 10.3 1.0
C E:VAL75 3.5 12.9 1.0
CG E:GLU80 3.7 11.8 1.0
OE2 E:GLU70 3.8 12.1 1.0
CG E:GLU77 3.8 17.6 1.0
N E:GLU77 4.0 17.6 1.0
CA E:ILE73 4.2 11.5 1.0
N E:VAL75 4.3 12.4 1.0
CB E:GLU77 4.3 17.0 1.0
N E:ILE73 4.3 10.9 1.0
N E:ASN72 4.3 10.1 1.0
OE2 E:GLU77 4.3 18.5 1.0
CA E:LEU76 4.4 14.0 1.0
N E:LEU76 4.4 11.3 1.0
OE1 E:GLU80 4.4 13.8 1.0
CA E:ASN72 4.5 10.4 1.0
CA E:VAL75 4.5 12.6 1.0
C E:ILE73 4.5 11.7 1.0
O E:HOH565 4.5 25.6 1.0
CG E:GLU70 4.6 9.1 1.0
N E:HIS71 4.6 12.0 1.0
C E:LEU76 4.6 16.2 1.0
CB E:ASN72 4.8 11.2 1.0
CA E:GLU77 4.8 18.7 1.0
CA E:GLU70 4.8 10.2 1.0
CB E:GLU70 4.8 8.4 1.0
N E:ASN74 4.9 10.9 1.0
O E:ILE73 4.9 11.7 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: Thu Jul 11 08:18:44 2024

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