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Calcium in PDB 1qi4: Mutant (E219G) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose

Enzymatic activity of Mutant (E219G) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose

All present enzymatic activity of Mutant (E219G) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose:
3.2.1.60;

Protein crystallography data

The structure of Mutant (E219G) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose, PDB code: 1qi4 was solved by K.Hasegawa, M.Kubota, Y.Matsuura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 65.520, 171.100, 46.970, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Mutant (E219G) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose (pdb code 1qi4). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Mutant (E219G) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose, PDB code: 1qi4:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1qi4

Go back to Calcium Binding Sites List in 1qi4
Calcium binding site 1 out of 2 in the Mutant (E219G) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Mutant (E219G) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca451

b:19.7
occ:1.00
OD2 A:ASP162 2.3 15.0 1.0
O A:HOH553 2.4 12.9 1.0
O A:GLY197 2.4 14.8 1.0
OD1 A:ASN116 2.4 14.8 1.0
O A:ASP154 2.5 16.4 1.0
OD2 A:ASP151 2.5 18.5 1.0
OD1 A:ASP151 2.6 19.7 1.0
CG A:ASP151 2.8 19.2 1.0
CG A:ASP162 3.4 15.6 1.0
C A:GLY197 3.5 14.9 1.0
CG A:ASN116 3.5 13.6 1.0
C A:ASP154 3.6 17.0 1.0
CA A:GLY197 3.8 14.7 1.0
ND2 A:ASN116 4.0 12.2 1.0
CB A:ASP162 4.1 16.3 1.0
C A:GLY153 4.1 18.2 1.0
CA A:ARG155 4.2 18.2 1.0
O A:GLY153 4.2 18.6 1.0
CB A:ASP151 4.3 19.5 1.0
N A:ARG155 4.4 17.1 1.0
N A:ASP154 4.4 17.9 1.0
OD1 A:ASP162 4.5 14.6 1.0
O A:HOH525 4.5 16.5 1.0
NH1 A:ARG137 4.5 20.2 1.0
O A:ASN116 4.5 15.9 1.0
CA A:GLY153 4.6 18.3 1.0
N A:TYR198 4.7 14.9 1.0
O A:LEU163 4.7 21.2 1.0
CA A:ASP154 4.7 17.2 1.0
N A:GLY153 4.7 19.0 1.0
CB A:ASN116 4.8 14.1 1.0

Calcium binding site 2 out of 2 in 1qi4

Go back to Calcium Binding Sites List in 1qi4
Calcium binding site 2 out of 2 in the Mutant (E219G) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Mutant (E219G) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca452

b:17.5
occ:1.00
OD1 A:ASP1 1.8 47.3 1.0
OE2 A:GLU17 2.0 17.6 1.0
O A:HIS13 2.2 17.0 1.0
OD1 A:ASP16 2.3 19.8 1.0
O A:GLN2 2.4 41.7 1.0
ND1 A:HIS13 2.4 20.9 1.0
CG A:ASP1 2.9 47.8 1.0
CD A:GLU17 3.1 16.7 1.0
CE1 A:HIS13 3.3 20.6 1.0
C A:HIS13 3.3 16.8 1.0
CG A:ASP16 3.4 20.2 1.0
OD2 A:ASP1 3.5 49.3 1.0
CG A:HIS13 3.5 19.8 1.0
C A:GLN2 3.6 42.0 1.0
OD2 A:ASP16 3.7 22.1 1.0
CB A:HIS13 3.9 18.4 1.0
CG A:GLU17 3.9 14.5 1.0
N A:GLN2 4.1 45.2 1.0
OE1 A:GLU17 4.2 16.3 1.0
N A:GLY14 4.2 16.4 1.0
CB A:ASP1 4.2 47.4 1.0
CA A:HIS13 4.2 17.2 1.0
CA A:GLY14 4.2 16.6 1.0
CE A:LYS108 4.3 21.8 1.0
C A:ASP1 4.3 46.2 1.0
CA A:ALA3 4.4 37.6 1.0
NE2 A:HIS13 4.4 20.9 1.0
NZ A:LYS108 4.5 21.2 1.0
CA A:GLN2 4.5 44.0 1.0
CA A:ASP1 4.5 46.6 1.0
N A:ALA3 4.5 40.0 1.0
CD2 A:HIS13 4.6 20.2 1.0
N A:ASP16 4.7 16.9 1.0
CB A:ASP16 4.7 17.4 1.0
N A:GLU17 4.7 16.4 1.0
C A:ASP16 4.8 16.7 1.0
O A:ASP1 4.8 46.8 1.0
C A:GLY14 4.8 17.0 1.0
CB A:GLN2 4.9 47.3 1.0
N A:GLY15 5.0 17.0 1.0
CA A:ASP16 5.0 16.6 1.0

Reference:

K.Hasegawa, M.Kubota, Y.Matsuura. Roles of Catalytic Residues in Alpha-Amylases As Evidenced By the Structures of the Product-Complexed Mutants of A Maltotetraose-Forming Amylase. Protein Eng. V. 12 819 1999.
ISSN: ISSN 0269-2139
PubMed: 10556241
DOI: 10.1093/PROTEIN/12.10.819
Page generated: Thu Jul 11 21:47:55 2024

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