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Calcium in PDB 1tmq: Structure of Tenebrio Molitor Larval Alpha-Amylase in Complex with Ragi Bifunctional Inhibitor

Enzymatic activity of Structure of Tenebrio Molitor Larval Alpha-Amylase in Complex with Ragi Bifunctional Inhibitor

All present enzymatic activity of Structure of Tenebrio Molitor Larval Alpha-Amylase in Complex with Ragi Bifunctional Inhibitor:
3.2.1.1;

Protein crystallography data

The structure of Structure of Tenebrio Molitor Larval Alpha-Amylase in Complex with Ragi Bifunctional Inhibitor, PDB code: 1tmq was solved by F.X.Gomis-Rueth, S.Strobl, R.Glockshuber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 2.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 79.160, 186.870, 111.540, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 26.1

Other elements in 1tmq:

The structure of Structure of Tenebrio Molitor Larval Alpha-Amylase in Complex with Ragi Bifunctional Inhibitor also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of Tenebrio Molitor Larval Alpha-Amylase in Complex with Ragi Bifunctional Inhibitor (pdb code 1tmq). 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 Structure of Tenebrio Molitor Larval Alpha-Amylase in Complex with Ragi Bifunctional Inhibitor, PDB code: 1tmq:

Calcium binding site 1 out of 1 in 1tmq

Go back to Calcium Binding Sites List in 1tmq
Calcium binding site 1 out of 1 in the Structure of Tenebrio Molitor Larval Alpha-Amylase in Complex with Ragi Bifunctional Inhibitor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Tenebrio Molitor Larval Alpha-Amylase in Complex with Ragi Bifunctional Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1001

b:17.8
occ:1.00
 O A:HOH5011 2.1 23.8 1.0
O A:ARG146 2.3 17.9 1.0
O A:HIS189 2.4 14.4 1.0
OD1 A:ASN98 2.4 17.4 1.0
OD2 A:ASP155 2.5 18.2 1.0
O A:HOH1049 2.6 19.4 1.0
OD1 A:ASP155 2.7 16.5 1.0
CG A:ASP155 2.9 14.8 1.0
C A:ARG146 3.5 15.8 1.0
CG A:ASN98 3.6 10.2 1.0
C A:HIS189 3.6 12.1 1.0
ND2 A:ASN98 4.1 13.6 1.0
CA A:ARG146 4.2 15.4 1.0
CB A:HIS189 4.2 12.8 1.0
O A:ASN98 4.3 13.3 1.0
CB A:ASP155 4.4 13.2 1.0
ND1 A:HIS131 4.5 14.4 1.0
CA A:HIS189 4.5 11.4 1.0
CG A:MET190 4.5 9.5 1.0
O A:LEU156 4.5 16.0 1.0
N A:ASN147 4.5 16.6 1.0
O A:CYS148 4.5 15.8 1.0
N A:MET190 4.6 12.4 1.0
CE1 A:HIS131 4.6 15.3 1.0
CA A:MET190 4.6 12.2 1.0
CA A:ASN147 4.7 16.9 1.0
OE1 A:GLN158 4.7 13.8 1.0
O A:VAL145 4.8 16.4 1.0
CB A:ASN98 4.8 9.3 1.0
CB A:ARG146 4.9 14.7 1.0

Reference:

S.Strobl, K.Maskos, G.Wiegand, R.Huber, F.X.Gomis-Ruth, R.Glockshuber. A Novel Strategy For Inhibition of Alpha-Amylases: Yellow Meal Worm Alpha-Amylase in Complex with the Ragi Bifunctional Inhibitor at 2.5 A Resolution. Structure V. 6 911 1998.
ISSN: ISSN 0969-2126
PubMed: 9687373
DOI: 10.1016/S0969-2126(98)00092-6
Page generated: Thu Jul 11 23:08:46 2024

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