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Calcium in PDB 1e3x: Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.92A

Enzymatic activity of Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.92A

All present enzymatic activity of Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.92A:
3.2.1.1;

Protein crystallography data

The structure of Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.92A, PDB code: 1e3x was solved by A.M.Brzozowski, D.M.Lawson, J.P.Turkenburg, H.Bisgaard-Frantzen, A.Svendsen, T.V.Borchert, Z.Dauter, K.S.Wilson, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 53.000, 78.200, 240.600, 90.00, 90.00, 90.00
R / Rfree (%) 14 / 20

Other elements in 1e3x:

The structure of Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.92A also contains other interesting chemical elements:

Sodium (Na) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.92A (pdb code 1e3x). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.92A, PDB code: 1e3x:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in 1e3x

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Calcium binding site 1 out of 4 in the Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.92A


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.92A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca501

b:7.0
occ:1.00
 OD1 A:ASP200 2.3 6.2 1.0
O A:ASP194 2.4 8.2 1.0
OD1 A:ASN102 2.4 7.3 1.0
OD1 A:ASP194 2.4 6.5 1.0
O A:HOH2204 2.5 9.1 1.0
O A:HIS235 2.5 8.2 1.0
CG A:ASP200 3.1 6.0 1.0
OD2 A:ASP200 3.1 7.3 1.0
C A:ASP194 3.3 8.6 1.0
CG A:ASP194 3.5 9.7 1.0
CG A:ASN102 3.5 7.7 1.0
C A:HIS235 3.7 8.2 1.0
CA A:ASP194 3.8 8.9 1.0
O A:HOH2343 3.8 9.3 1.0
NA A:NA505 4.0 7.5 1.0
O A:ASN102 4.1 6.5 1.0
CB A:HIS235 4.1 6.7 1.0
ND2 A:ASN102 4.2 5.5 1.0
CB A:ASP194 4.2 7.9 1.0
OD2 A:ASP194 4.3 7.0 1.0
N A:TYR195 4.4 6.3 1.0
CA A:HIS235 4.4 8.6 1.0
O A:HOH2366 4.5 7.7 1.0
CB A:ASP200 4.6 5.1 1.0
N A:ILE236 4.6 6.3 1.0
CB A:ASN102 4.6 6.1 1.0
CA A:ILE236 4.7 6.2 1.0
O A:VAL201 4.8 7.0 1.0
CA A:ASN102 4.8 6.6 1.0
CG1 A:ILE236 4.8 6.5 1.0
CA A:TYR195 4.8 7.8 1.0
C A:ASN102 4.8 6.7 1.0

Calcium binding site 2 out of 4 in 1e3x

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Calcium binding site 2 out of 4 in the Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.92A


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.92A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca502

b:7.7
occ:1.00
 OD1 A:ASP183 2.3 6.7 1.0
OD1 A:ASP202 2.4 5.9 1.0
O A:ALA181 2.5 7.1 1.0
OD2 A:ASP204 2.5 11.5 1.0
OD1 A:ASP159 2.5 7.3 1.0
OD2 A:ASP159 2.6 6.1 1.0
O A:HOH2367 2.6 6.8 1.0
CG A:ASP159 2.9 8.0 1.0
CG A:ASP202 3.2 8.0 1.0
CG A:ASP204 3.4 12.3 1.0
CG A:ASP183 3.5 9.2 1.0
C A:ALA181 3.7 9.6 1.0
OD2 A:ASP202 3.7 7.6 1.0
N A:ASP183 3.9 7.6 1.0
CB A:ASP204 3.9 11.2 1.0
C A:TRP182 4.0 9.3 1.0
OD2 A:ASP183 4.1 8.2 1.0
CB A:ASP202 4.2 7.3 1.0
N A:ALA181 4.2 10.9 1.0
CA A:ASP183 4.3 7.5 1.0
CA A:ASP202 4.3 6.7 1.0
N A:ASP204 4.4 9.5 1.0
OD1 A:ASP204 4.4 12.9 1.0
CB A:ASP159 4.4 6.4 1.0
CA A:TRP182 4.4 7.8 1.0
CB A:ASP183 4.5 7.4 1.0
NA A:NA505 4.5 7.5 1.0
O A:TRP182 4.5 9.7 1.0
N A:TRP182 4.6 8.6 1.0
CA A:ALA181 4.6 9.7 1.0
O A:HOH2341 4.7 41.7 1.0
C A:ASP202 4.7 7.5 1.0
N A:TYR203 4.7 7.3 1.0
CA A:ASP204 4.7 10.1 1.0
O A:HOH2306 4.9 18.6 1.0
OD2 A:ASP194 4.9 7.0 1.0

Calcium binding site 3 out of 4 in 1e3x

Go back to Calcium Binding Sites List in 1e3x
Calcium binding site 3 out of 4 in the Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.92A


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.92A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca503

b:13.5
occ:1.00
 OE2 A:GLU447 2.4 11.8 1.0
OD1 A:ASN444 2.4 13.2 1.0
O A:HOH2619 2.5 14.1 1.0
O A:HOH2618 2.5 17.1 1.0
OE1 A:GLU447 2.6 12.2 1.0
O A:HOH2635 2.6 20.2 1.0
O A:HOH2679 2.6 18.9 1.0
O A:HOH2615 2.7 53.1 1.0
CD A:GLU447 2.9 13.9 1.0
CG A:ASN444 3.5 14.0 1.0
CB A:ASN444 4.1 14.7 1.0
CA A:ASN444 4.3 16.3 1.0
O A:SER422 4.3 14.2 1.0
CG A:GLU447 4.4 12.3 1.0
OE1 A:GLN482 4.4 24.1 1.0
ND2 A:ASN444 4.6 14.6 1.0
O A:GLN443 4.7 18.3 1.0
O A:HOH2638 4.8 40.2 1.0
CA A:ASN421 4.8 15.5 1.0
O A:HOH2617 4.8 47.5 1.0
OD1 A:ASN421 4.9 21.9 1.0
NE1 A:TRP449 5.0 12.4 1.0

Calcium binding site 4 out of 4 in 1e3x

Go back to Calcium Binding Sites List in 1e3x
Calcium binding site 4 out of 4 in the Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.92A


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Native Structure of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 1.92A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca504

b:14.6
occ:1.00
 O A:TYR302 2.3 14.1 1.0
OD1 A:ASP407 2.4 14.7 1.0
O A:GLY300 2.4 16.7 1.0
OD2 A:ASP430 2.5 11.7 1.0
OD1 A:ASP430 2.5 12.5 1.0
O A:HIS406 2.5 11.6 1.0
O A:HOH2488 2.6 15.2 1.0
CG A:ASP430 2.9 12.5 1.0
C A:GLY300 3.5 16.4 1.0
C A:HIS406 3.5 13.0 1.0
CG A:ASP407 3.5 14.8 1.0
C A:TYR302 3.6 15.0 1.0
CA A:ASP407 3.8 12.3 1.0
N A:TYR302 3.9 16.5 1.0
N A:ASP407 4.1 12.1 1.0
C A:GLY301 4.1 17.3 1.0
CB A:ASP407 4.1 13.5 1.0
CG A:MET304 4.3 12.7 1.0
CA A:GLY300 4.3 15.5 1.0
CA A:TYR302 4.3 15.2 1.0
N A:GLY301 4.3 15.7 1.0
CB A:ASP430 4.4 10.6 1.0
CA A:GLY301 4.4 17.1 1.0
OD2 A:ASP407 4.5 16.3 1.0
CB A:HIS406 4.5 18.2 1.0
N A:ASP303 4.5 14.6 1.0
N A:MET304 4.6 14.2 1.0
CD2 A:HIS406 4.6 22.3 1.0
CA A:HIS406 4.6 14.8 1.0
O A:GLY301 4.6 17.1 1.0
O A:HOH2599 4.6 44.8 1.0
CA A:ASP303 4.6 16.0 1.0
O A:HOH2205 4.7 46.8 1.0
O A:HOH2489 4.7 30.4 1.0
O A:HOH2480 4.8 14.7 1.0
CB A:TYR302 4.9 14.0 1.0
CG A:HIS406 4.9 20.7 1.0

Reference:

A.M.Brzozowski, D.M.Lawson, J.P.Turkenburg, H.Bisgaard-Frantzen, A.Svendsen, T.V.Borchert, Z.Dauter, K.S.Wilson, G.J.Davies. Structural Analysis of A Chimeric Bacterial Alpha-Amylase. High Resolution Analysis of Native and Ligand Complexes Biochemistry V. 39 9099 2000.
ISSN: ISSN 0006-2960
PubMed: 10924103
DOI: 10.1021/BI0000317
Page generated: Thu Jul 11 07:44:49 2024

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