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Calcium in PDB 1wp6: Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707.

Enzymatic activity of Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707.

All present enzymatic activity of Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707.:
3.2.1.98;

Protein crystallography data

The structure of Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707., PDB code: 1wp6 was solved by R.Kanai, K.Haga, T.Akiba, K.Yamane, K.Harata, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.620, 82.800, 127.170, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 21

Other elements in 1wp6:

The structure of Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707. also contains other interesting chemical elements:

Sodium (Na) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707. (pdb code 1wp6). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707., PDB code: 1wp6:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in 1wp6

Go back to Calcium Binding Sites List in 1wp6
Calcium binding site 1 out of 3 in the Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707.


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 Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca501

b:20.3
occ:1.00
OD1 A:ASP207 2.2 14.8 1.0
OD1 A:ASP188 2.4 21.8 1.0
O A:ALA186 2.4 20.4 1.0
OD2 A:ASP209 2.4 21.4 1.0
O A:HOH794 2.5 27.3 1.0
OD2 A:ASP163 2.5 20.1 1.0
OD1 A:ASP163 2.6 20.4 1.0
CG A:ASP163 2.9 19.9 1.0
CG A:ASP207 3.1 17.9 1.0
CG A:ASP209 3.3 21.6 1.0
CG A:ASP188 3.4 22.1 1.0
C A:ALA186 3.6 19.5 1.0
CB A:ASP209 3.7 21.8 1.0
OD2 A:ASP207 3.7 15.6 1.0
N A:ASP188 3.9 18.9 1.0
OD2 A:ASP188 4.0 19.2 1.0
C A:TRP187 4.1 19.6 1.0
CB A:ASP207 4.1 17.4 1.0
N A:ALA186 4.2 18.7 1.0
CA A:ASP188 4.3 18.8 1.0
OD1 A:ASP209 4.3 20.7 1.0
CB A:ASP163 4.3 19.2 1.0
N A:ASP209 4.3 21.9 1.0
CA A:ASP207 4.4 17.3 1.0
CB A:ASP188 4.4 18.1 1.0
NA A:NA504 4.4 24.5 1.0
O A:TRP187 4.5 19.6 1.0
CA A:TRP187 4.5 18.1 1.0
N A:TRP187 4.5 18.0 1.0
CA A:ALA186 4.5 20.0 1.0
CA A:ASP209 4.7 22.0 1.0
O A:HOH647 4.7 30.2 1.0
N A:MET208 4.7 18.6 1.0
C A:ASP207 4.8 18.1 1.0
O A:GLY184 4.8 18.3 1.0
OD2 A:ASP199 5.0 18.7 1.0

Calcium binding site 2 out of 3 in 1wp6

Go back to Calcium Binding Sites List in 1wp6
Calcium binding site 2 out of 3 in the Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca502

b:17.7
occ:1.00
OD1 A:ASN106 2.3 20.6 1.0
O A:ASP199 2.3 16.1 1.0
OD1 A:ASP199 2.4 17.6 1.0
OD1 A:ASP205 2.4 19.9 1.0
O A:HIS240 2.4 17.0 1.0
O A:HOH637 2.5 15.3 1.0
OD2 A:ASP205 2.9 21.1 1.0
CG A:ASP205 3.0 19.5 1.0
C A:ASP199 3.3 16.5 1.0
CG A:ASN106 3.4 19.8 1.0
CG A:ASP199 3.4 17.6 1.0
C A:HIS240 3.6 18.4 1.0
O A:HOH638 3.7 18.7 1.0
CA A:ASP199 3.8 16.7 1.0
NA A:NA504 4.0 24.5 1.0
ND2 A:ASN106 4.0 19.8 1.0
CB A:HIS240 4.1 16.0 1.0
O A:ASN106 4.1 18.9 1.0
CB A:ASP199 4.2 17.1 1.0
OD2 A:ASP199 4.2 18.7 1.0
CA A:HIS240 4.4 16.9 1.0
N A:TYR200 4.4 17.4 1.0
CB A:ASP205 4.5 18.5 1.0
N A:ILE241 4.5 16.3 1.0
CB A:ASN106 4.6 19.7 1.0
O A:ILE206 4.6 19.3 1.0
O A:HOH639 4.7 16.0 1.0
CA A:ILE241 4.7 16.4 1.0
CA A:TYR200 4.7 18.5 1.0
CA A:ASN106 4.8 19.2 1.0
C A:ASN106 4.8 19.4 1.0
CG1 A:ILE241 5.0 16.5 1.0

Calcium binding site 3 out of 3 in 1wp6

Go back to Calcium Binding Sites List in 1wp6
Calcium binding site 3 out of 3 in the Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp.707. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca503

b:20.1
occ:1.00
OD1 A:ASN409 2.2 20.4 1.0
O A:GLY305 2.3 19.6 1.0
O A:TYR307 2.4 17.4 1.0
O A:HOH687 2.4 19.7 1.0
O A:HIS408 2.5 20.0 1.0
OD1 A:ASP432 2.5 20.8 1.0
OD2 A:ASP432 2.6 20.1 1.0
CG A:ASP432 2.9 21.9 1.0
C A:GLY305 3.4 18.5 1.0
CG A:ASN409 3.4 21.7 1.0
C A:HIS408 3.5 18.5 1.0
C A:TYR307 3.5 16.8 1.0
N A:TYR307 3.8 16.9 1.0
CA A:ASN409 3.8 19.9 1.0
C A:ASN306 4.0 18.0 1.0
N A:ASN409 4.0 18.4 1.0
CB A:ASN409 4.1 19.8 1.0
N A:ASN306 4.1 18.9 1.0
CA A:ASN306 4.2 18.8 1.0
CG A:MET309 4.2 17.4 1.0
CA A:GLY305 4.3 17.5 1.0
CA A:TYR307 4.3 17.6 1.0
ND1 A:HIS408 4.4 23.5 1.0
O A:HOH780 4.4 24.5 1.0
ND2 A:ASN409 4.4 22.0 1.0
N A:MET309 4.4 17.1 1.0
CB A:ASP432 4.4 19.6 1.0
N A:ASP308 4.5 18.4 1.0
O A:HOH689 4.5 24.5 1.0
O A:ASN306 4.6 19.1 1.0
O A:HOH881 4.6 36.1 1.0
CA A:ASP308 4.6 17.0 1.0
CA A:HIS408 4.7 18.8 1.0
CB A:HIS408 4.7 19.6 1.0
O A:HOH684 4.8 19.3 1.0
CB A:TYR307 4.8 18.6 1.0
CB A:MET309 5.0 18.0 1.0

Reference:

R.Kanai, K.Haga, T.Akiba, K.Yamane, K.Harata. Biochemical and Crystallographic Analyses of Maltohexaose-Producing Amylase From Alkalophilic Bacillus Sp. 707 Biochemistry V. 43 14047 2004.
ISSN: ISSN 0006-2960
PubMed: 15518553
DOI: 10.1021/BI048489M
Page generated: Sat Dec 12 03:26:04 2020

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