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Calcium in PDB 3voc: Crystal Structure of the Catalytic Domain of Beta-Amylase From Paenibacillus Polymyxa

Enzymatic activity of Crystal Structure of the Catalytic Domain of Beta-Amylase From Paenibacillus Polymyxa

All present enzymatic activity of Crystal Structure of the Catalytic Domain of Beta-Amylase From Paenibacillus Polymyxa:
3.2.1.2;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of Beta-Amylase From Paenibacillus Polymyxa, PDB code: 3voc was solved by S.Nishimura, T.Fujioka, T.Nakaniwa, T.Tada, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.00 / 1.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 61.028, 68.519, 93.904, 90.00, 90.00, 90.00
R / Rfree (%) 15.3 / 19

Other elements in 3voc:

The structure of Crystal Structure of the Catalytic Domain of Beta-Amylase From Paenibacillus Polymyxa also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Catalytic Domain of Beta-Amylase From Paenibacillus Polymyxa (pdb code 3voc). 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 Catalytic Domain of Beta-Amylase From Paenibacillus Polymyxa, PDB code: 3voc:

Calcium binding site 1 out of 1 in 3voc

Go back to Calcium Binding Sites List in 3voc
Calcium binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of Beta-Amylase From Paenibacillus Polymyxa


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 Catalytic Domain of Beta-Amylase From Paenibacillus Polymyxa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca501

b:17.5
occ:1.00
 OE1 A:GLU135 2.2 15.9 1.0
OD1 A:ASP52 2.3 17.4 1.0
OE1 A:GLN132 2.3 16.9 1.0
O A:HOH1046 2.3 15.0 1.0
OE2 A:GLU48 2.4 16.6 1.0
OD1 A:ASN53 2.4 18.3 1.0
CD A:GLN132 3.3 18.9 1.0
CD A:GLU135 3.3 17.1 1.0
CD A:GLU48 3.4 17.0 1.0
CG A:ASN53 3.4 18.8 1.0
CG A:ASP52 3.5 20.2 1.0
OE1 A:GLU48 3.7 16.0 1.0
N A:ASN53 3.7 18.5 1.0
NE2 A:GLN132 3.7 20.8 1.0
CB A:GLU135 3.9 16.2 1.0
CH2 A:TRP98 4.1 17.1 1.0
ND2 A:ASN53 4.1 21.0 1.0
OE2 A:GLU135 4.1 18.7 1.0
OD2 A:ASP52 4.2 21.9 1.0
CG A:GLU135 4.2 16.3 1.0
CA A:ASN53 4.3 18.4 1.0
C A:ASP52 4.4 18.6 1.0
CB A:ASN53 4.4 18.6 1.0
O A:HOH1200 4.4 22.6 1.0
CA A:ASP52 4.5 19.0 1.0
O A:GLN132 4.5 16.5 1.0
CB A:ASP52 4.6 18.7 1.0
CA A:GLN132 4.6 16.4 1.0
CG A:GLN132 4.6 17.7 1.0
CZ2 A:TRP98 4.7 17.9 1.0
CG A:GLU48 4.7 15.2 1.0
CB A:GLN132 4.8 16.8 1.0
CZ A:PHE55 4.8 16.4 1.0
CZ3 A:TRP98 4.9 17.3 1.0

Reference:

S.Nishimura, T.Fujioka, R.Takahashi, T.Nakaniwa, H.Fukada, T.Inui, T.Tada, T.Kawaguchi, J.Sumitani. Structural Analysis By X-Ray Crystallography and Small-Angle Scattering of the Multi-Domain Beta-Amylase From Paenibacillus Polymyxa To Be Published.
Page generated: Tue Jul 8 17:40:03 2025

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