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Calcium in PDB 1vep: Crystal Structure Analysis of Triple (T47M/Y164E/T328N) /Maltose of Bacillus Cereus Beta-Amylase at pH 6.5

Enzymatic activity of Crystal Structure Analysis of Triple (T47M/Y164E/T328N) /Maltose of Bacillus Cereus Beta-Amylase at pH 6.5

All present enzymatic activity of Crystal Structure Analysis of Triple (T47M/Y164E/T328N) /Maltose of Bacillus Cereus Beta-Amylase at pH 6.5:
3.2.1.2;

Protein crystallography data

The structure of Crystal Structure Analysis of Triple (T47M/Y164E/T328N) /Maltose of Bacillus Cereus Beta-Amylase at pH 6.5, PDB code: 1vep was solved by A.Hirata, M.Adachi, S.Utsumi, B.Mikami, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.90 / 2.06
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 57.450, 92.695, 65.755, 90.00, 102.37, 90.00
R / Rfree (%) 18.3 / 22.6

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure Analysis of Triple (T47M/Y164E/T328N) /Maltose of Bacillus Cereus Beta-Amylase at pH 6.5 (pdb code 1vep). 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 Analysis of Triple (T47M/Y164E/T328N) /Maltose of Bacillus Cereus Beta-Amylase at pH 6.5, PDB code: 1vep:

Calcium binding site 1 out of 1 in 1vep

Go back to Calcium Binding Sites List in 1vep
Calcium binding site 1 out of 1 in the Crystal Structure Analysis of Triple (T47M/Y164E/T328N) /Maltose of Bacillus Cereus Beta-Amylase at pH 6.5


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure Analysis of Triple (T47M/Y164E/T328N) /Maltose of Bacillus Cereus Beta-Amylase at pH 6.5 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca930

b:42.7
occ:1.00
OD1 A:ASP60 2.3 38.6 1.0
OE1 A:GLU141 2.6 27.6 1.0
OE1 A:GLU144 2.6 30.4 1.0
OE2 A:GLU56 2.6 25.2 1.0
O A:HOH757 2.7 22.2 1.0
OE1 A:GLN61 2.8 43.2 1.0
CG A:ASP60 3.4 36.9 1.0
CD A:GLU56 3.6 27.3 1.0
CD A:GLU141 3.7 26.8 1.0
CD A:GLU144 3.7 27.1 1.0
OE1 A:GLU56 3.8 24.7 1.0
N A:GLN61 3.8 32.4 1.0
CD A:GLN61 3.8 42.3 1.0
NZ A:LYS140 3.9 28.8 1.0
CH2 A:TRP106 4.0 34.0 1.0
CB A:GLU144 4.0 22.4 1.0
OE2 A:GLU141 4.1 29.8 1.0
OD2 A:ASP60 4.1 40.0 1.0
CG A:GLN61 4.3 39.6 1.0
CA A:ASP60 4.4 34.1 1.0
CG A:GLU144 4.4 25.5 1.0
CB A:ASP60 4.4 34.4 1.0
CZ A:PHE63 4.5 22.9 1.0
OE2 A:GLU144 4.5 30.1 1.0
C A:ASP60 4.5 33.1 1.0
CA A:GLU141 4.5 20.3 1.0
CA A:GLN61 4.6 34.0 1.0
CZ3 A:TRP106 4.7 33.7 1.0
O A:GLU141 4.8 19.7 1.0
CZ2 A:TRP106 4.8 32.9 1.0
CG A:GLU141 4.9 24.6 1.0
NE2 A:GLN61 4.9 43.4 1.0
CG A:GLU56 4.9 28.8 1.0
CB A:GLU141 4.9 20.5 1.0
CE1 A:PHE63 5.0 23.0 1.0

Reference:

A.Hirata, M.Adachi, S.Utsumi, B.Mikami. Engineering of the pH Optimum of Bacillus Cereus Beta-Amylase: Conversion of the pH Optimum From A Bacterial Type to A Higher-Plant Type Biochemistry V. 43 12523 2004.
ISSN: ISSN 0006-2960
PubMed: 15449941
DOI: 10.1021/BI049173H
Page generated: Sat Dec 12 03:24:56 2020

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