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Calcium in PDB 1e40: Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A

Enzymatic activity of Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A

All present enzymatic activity of Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A:
3.2.1.1;

Protein crystallography data

The structure of Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A, PDB code: 1e40 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 / 2.20
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 52.720, 78.270, 238.860, 90.00, 90.00, 90.00
R / Rfree (%) 13 / 21

Other elements in 1e40:

The structure of Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A also contains other interesting chemical elements:

Sodium (Na) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A (pdb code 1e40). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A, PDB code: 1e40:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in 1e40

Go back to Calcium Binding Sites List in 1e40
Calcium binding site 1 out of 4 in the Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca501

b:8.1
occ:1.00
 OD1 A:ASN102 2.2 5.3 1.0
OD1 A:ASP194 2.4 7.3 1.0
O A:HIS235 2.4 10.1 1.0
O A:ASP194 2.4 7.8 1.0
OD1 A:ASP200 2.4 7.0 1.0
O A:HOH2151 2.5 8.1 1.0
CG A:ASP200 3.2 6.4 1.0
OD2 A:ASP200 3.2 6.0 1.0
C A:ASP194 3.3 7.2 1.0
CG A:ASN102 3.4 6.2 1.0
CG A:ASP194 3.4 8.6 1.0
C A:HIS235 3.6 10.3 1.0
O A:HOH2275 3.7 7.9 1.0
CA A:ASP194 3.8 7.8 1.0
CB A:HIS235 4.0 9.2 1.0
O A:ASN102 4.1 6.8 1.0
NA A:NA505 4.1 9.1 1.0
ND2 A:ASN102 4.1 4.8 1.0
CB A:ASP194 4.2 7.1 1.0
OD2 A:ASP194 4.3 7.5 1.0
CA A:HIS235 4.4 10.6 1.0
N A:TYR195 4.4 7.5 1.0
O A:HOH2278 4.5 7.2 1.0
N A:ILE236 4.5 8.8 1.0
CB A:ASN102 4.6 6.1 1.0
CB A:ASP200 4.6 5.9 1.0
CA A:ILE236 4.7 8.7 1.0
CG1 A:ILE236 4.8 7.2 1.0
CA A:TYR195 4.8 8.6 1.0
O A:VAL201 4.8 5.6 1.0
CA A:ASN102 4.8 7.0 1.0
C A:ASN102 4.8 7.0 1.0

Calcium binding site 2 out of 4 in 1e40

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Calcium binding site 2 out of 4 in the Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca502

b:8.3
occ:1.00
 OD1 A:ASP183 2.2 8.1 1.0
O A:ALA181 2.3 10.0 1.0
OD1 A:ASP202 2.4 6.1 1.0
OD2 A:ASP204 2.5 9.9 1.0
OD2 A:ASP159 2.5 5.7 1.0
OD1 A:ASP159 2.6 8.0 1.0
O A:HOH2256 2.8 7.8 1.0
CG A:ASP159 2.9 6.8 1.0
CG A:ASP202 3.2 7.8 1.0
CG A:ASP183 3.3 8.3 1.0
CG A:ASP204 3.4 9.5 1.0
C A:ALA181 3.5 9.4 1.0
N A:ASP183 3.8 9.2 1.0
OD2 A:ASP202 3.8 8.3 1.0
CB A:ASP204 3.9 8.5 1.0
OD2 A:ASP183 3.9 7.1 1.0
C A:TRP182 4.1 9.6 1.0
N A:ALA181 4.2 11.9 1.0
CA A:ASP183 4.2 8.4 1.0
CB A:ASP202 4.2 7.1 1.0
CA A:ASP202 4.3 6.7 1.0
OD1 A:ASP204 4.3 8.7 1.0
N A:ASP204 4.3 8.2 1.0
CB A:ASP159 4.4 5.0 1.0
CB A:ASP183 4.4 7.7 1.0
N A:TRP182 4.4 9.2 1.0
CA A:TRP182 4.4 9.2 1.0
NA A:NA505 4.4 9.1 1.0
CA A:ALA181 4.5 10.0 1.0
O A:TRP182 4.6 9.1 1.0
N A:TYR203 4.6 6.0 1.0
C A:ASP202 4.7 7.2 1.0
CA A:ASP204 4.7 10.1 1.0
O A:HOH2258 4.8 34.4 1.0
OD2 A:ASP194 4.8 7.5 1.0
O A:HOH2257 5.0 18.8 1.0

Calcium binding site 3 out of 4 in 1e40

Go back to Calcium Binding Sites List in 1e40
Calcium binding site 3 out of 4 in the Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca503

b:17.1
occ:1.00
 OD1 A:ASN444 2.2 15.2 1.0
O A:HOH2476 2.5 14.0 1.0
OE2 A:GLU447 2.5 16.2 1.0
OE1 A:GLU447 2.6 14.0 1.0
O A:HOH2477 2.6 13.5 1.0
O A:HOH2530 2.8 19.2 1.0
CD A:GLU447 2.8 15.5 1.0
O A:HOH2490 2.9 23.7 1.0
O A:HOH2493 2.9 39.7 1.0
CG A:ASN444 3.3 15.7 1.0
CB A:ASN444 4.0 16.2 1.0
O A:SER422 4.3 14.3 1.0
CG A:GLU447 4.3 13.9 1.0
ND2 A:ASN444 4.3 15.5 1.0
OE1 A:GLN482 4.4 21.3 1.0
CA A:ASN444 4.4 17.2 1.0
O A:HOH2494 4.6 43.6 1.0
O A:HOH2475 4.7 54.5 1.0
CA A:ASN421 4.7 16.8 1.0
O A:GLN443 4.8 16.7 1.0
O A:HOH2463 4.8 33.8 1.0
NE1 A:TRP449 4.9 12.4 1.0
OD1 A:ASN421 4.9 22.0 1.0
CZ2 A:TRP449 5.0 13.4 1.0
C A:ASN421 5.0 14.9 1.0

Calcium binding site 4 out of 4 in 1e40

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Calcium binding site 4 out of 4 in the Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Tris/Maltotriose Complex of Chimaeric Amylase From B. Amyloliquefaciens and B. Licheniformis at 2.2A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca504

b:14.7
occ:1.00
 O A:TYR302 2.2 10.9 1.0
OD1 A:ASP407 2.3 16.4 1.0
O A:GLY300 2.4 14.9 1.0
O A:HIS406 2.5 11.4 1.0
OD2 A:ASP430 2.5 12.7 1.0
OD1 A:ASP430 2.5 11.7 1.0
O A:HOH2365 2.7 20.0 1.0
CG A:ASP430 2.8 12.4 1.0
C A:TYR302 3.4 12.6 1.0
CG A:ASP407 3.4 16.2 1.0
C A:HIS406 3.4 14.0 1.0
C A:GLY300 3.5 15.1 1.0
CA A:ASP407 3.7 14.9 1.0
N A:TYR302 3.8 14.7 1.0
N A:ASP407 4.0 14.9 1.0
CB A:ASP407 4.1 16.2 1.0
C A:GLY301 4.1 14.9 1.0
CA A:TYR302 4.2 13.4 1.0
CG A:MET304 4.2 13.1 1.0
CA A:GLY300 4.3 14.9 1.0
CB A:ASP430 4.3 12.0 1.0
N A:GLY301 4.4 12.6 1.0
N A:MET304 4.4 15.2 1.0
CA A:GLY301 4.4 14.0 1.0
OD2 A:ASP407 4.4 17.7 1.0
N A:ASP303 4.4 13.4 1.0
CD2 A:HIS406 4.4 19.9 1.0
O A:HOH2458 4.5 35.3 1.0
CB A:HIS406 4.5 17.3 1.0
CA A:HIS406 4.6 15.2 1.0
CA A:ASP303 4.6 14.5 1.0
O A:GLY301 4.6 13.8 1.0
CB A:TYR302 4.8 13.9 1.0
O A:HOH2366 4.8 32.9 1.0
O A:HOH2478 4.8 12.9 1.0
CG A:HIS406 4.9 19.3 1.0
O A:HOH2199 5.0 39.4 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 07:44:53 2024

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