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Calcium in PDB 1utj: Trypsin Specificity As Elucidated By Lie Calculations, X-Ray Structures and Association Constant Measurements

Enzymatic activity of Trypsin Specificity As Elucidated By Lie Calculations, X-Ray Structures and Association Constant Measurements

All present enzymatic activity of Trypsin Specificity As Elucidated By Lie Calculations, X-Ray Structures and Association Constant Measurements:
3.4.21.4;

Protein crystallography data

The structure of Trypsin Specificity As Elucidated By Lie Calculations, X-Ray Structures and Association Constant Measurements, PDB code: 1utj was solved by H.-K.S.Leiros, B.O.Brandsdal, O.A.Andersen, V.Os, I.Leiros, R.Helland, J.Otlewski, 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) 8 / 1.83
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.030, 48.180, 83.010, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 20.7

Calcium Binding Sites:

The binding sites of Calcium atom in the Trypsin Specificity As Elucidated By Lie Calculations, X-Ray Structures and Association Constant Measurements (pdb code 1utj). 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 Trypsin Specificity As Elucidated By Lie Calculations, X-Ray Structures and Association Constant Measurements, PDB code: 1utj:

Calcium binding site 1 out of 1 in 1utj

Go back to Calcium Binding Sites List in 1utj
Calcium binding site 1 out of 1 in the Trypsin Specificity As Elucidated By Lie Calculations, X-Ray Structures and Association Constant Measurements


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Trypsin Specificity As Elucidated By Lie Calculations, X-Ray Structures and Association Constant Measurements within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca247

b:6.5
occ:1.00
 O A:VAL75 2.2 6.9 1.0
O A:ASN72 2.3 7.0 1.0
OE1 A:GLU70 2.3 7.7 1.0
O A:HOH2018 2.4 8.3 1.0
OE2 A:GLU80 2.4 6.1 1.0
OE2 A:GLU77 2.4 9.5 1.0
H2 A:HOH2018 3.1 8.3 1.0
H1 A:HOH2018 3.2 8.3 1.0
CD A:GLU77 3.4 8.7 1.0
CD A:GLU70 3.4 8.6 1.0
C A:VAL75 3.4 11.9 1.0
CD A:GLU80 3.5 9.3 1.0
C A:ASN72 3.5 6.1 1.0
H A:GLU77 3.6 0.0 1.0
H A:HIS71 3.6 0.0 1.0
H A:VAL75 3.7 0.0 1.0
OE2 A:GLU70 3.7 7.9 1.0
CG A:GLU80 3.8 7.0 1.0
H A:ASN72 3.9 0.0 1.0
CG A:GLU77 3.9 8.3 1.0
N A:GLU77 4.1 7.9 1.0
N A:VAL75 4.2 13.4 1.0
CA A:THR76 4.2 10.5 1.0
CA A:ILE73 4.2 9.0 1.0
N A:THR76 4.2 10.1 1.0
OE1 A:GLU77 4.3 11.9 1.0
N A:ILE73 4.3 6.8 1.0
N A:ASN72 4.3 6.0 1.0
CA A:VAL75 4.4 12.6 1.0
CB A:GLU77 4.4 6.0 1.0
CA A:ASN72 4.4 5.6 1.0
C A:ILE73 4.5 10.4 1.0
N A:HIS71 4.5 6.0 1.0
C A:THR76 4.6 9.0 1.0
OE1 A:GLU80 4.6 6.8 1.0
CG A:GLU70 4.6 7.5 1.0
CA A:GLU70 4.8 4.9 1.0
CB A:ASN72 4.8 6.6 1.0
N A:LYS74 4.8 11.4 1.0
O A:ILE73 4.8 10.7 1.0
CB A:GLU70 4.9 6.8 1.0
H A:LYS74 4.9 0.0 1.0
CA A:GLU77 5.0 8.6 1.0

Reference:

H.-K.S.Leiros, B.O.Brandsdal, O.A.Andersen, V.Os, I.Leiros, R.Helland, J.Otlewski, N.P.Willassen, A.O.Smalas. Trypsin Specificity As Elucidated By Lie Calculations, X-Ray Structures, and Association Constant Measurements Protein Sci. V. 13 1056 2004.
ISSN: ISSN 0961-8368
PubMed: 15044735
DOI: 10.1110/PS.03498604
Page generated: Thu Jul 11 23:39:11 2024

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