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Calcium in PDB 1gcy: High Resolution Crystal Structure of Maltotetraose-Forming Exo-Amylase

Enzymatic activity of High Resolution Crystal Structure of Maltotetraose-Forming Exo-Amylase

All present enzymatic activity of High Resolution Crystal Structure of Maltotetraose-Forming Exo-Amylase:
3.2.1.60;

Protein crystallography data

The structure of High Resolution Crystal Structure of Maltotetraose-Forming Exo-Amylase, PDB code: 1gcy was solved by Y.Mezaki, Y.Katsuya, M.Kubota, Y.Matsuura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 69.420, 171.660, 46.350, 90.00, 90.00, 90.00
R / Rfree (%) 25.9 / 30.4

Calcium Binding Sites:

The binding sites of Calcium atom in the High Resolution Crystal Structure of Maltotetraose-Forming Exo-Amylase (pdb code 1gcy). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the High Resolution Crystal Structure of Maltotetraose-Forming Exo-Amylase, PDB code: 1gcy:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1gcy

Go back to Calcium Binding Sites List in 1gcy
Calcium binding site 1 out of 2 in the High Resolution Crystal Structure of Maltotetraose-Forming Exo-Amylase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of High Resolution Crystal Structure of Maltotetraose-Forming Exo-Amylase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca528

b:17.3
occ:1.00
O A:GLY197 2.3 19.7 1.0
OD1 A:ASP151 2.4 17.6 1.0
O A:ASP154 2.4 18.4 1.0
OD1 A:ASN116 2.4 11.4 1.0
OD1 A:ASP162 2.5 12.9 1.0
O A:HOH555 2.6 17.9 1.0
OD2 A:ASP151 2.8 17.1 1.0
CG A:ASP151 2.9 17.7 1.0
C A:GLY197 3.3 17.6 1.0
CG A:ASN116 3.5 10.7 1.0
CA A:GLY197 3.6 16.0 1.0
C A:ASP154 3.6 17.4 1.0
CG A:ASP162 3.7 11.8 1.0
ND2 A:ASN116 4.0 13.1 1.0
C A:GLY153 4.1 17.9 1.0
CA A:ARG155 4.2 17.9 1.0
O A:GLY153 4.2 19.2 1.0
CB A:ASP162 4.3 15.5 1.0
N A:ASP154 4.4 15.9 1.0
N A:ARG155 4.4 18.0 1.0
O A:ASN116 4.4 16.6 1.0
CB A:ASP151 4.4 14.8 1.0
O A:HOH715 4.5 18.9 1.0
N A:TYR198 4.5 16.1 1.0
CA A:GLY153 4.5 15.7 1.0
CA A:ASP154 4.7 17.4 1.0
O A:LEU163 4.7 19.5 1.0
NH1 A:ARG137 4.7 18.9 1.0
OD2 A:ASP162 4.7 15.4 1.0
CB A:ASN116 4.7 14.0 1.0
N A:GLY153 4.8 15.9 1.0
CA A:ASN116 5.0 16.6 1.0

Calcium binding site 2 out of 2 in 1gcy

Go back to Calcium Binding Sites List in 1gcy
Calcium binding site 2 out of 2 in the High Resolution Crystal Structure of Maltotetraose-Forming Exo-Amylase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of High Resolution Crystal Structure of Maltotetraose-Forming Exo-Amylase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca529

b:21.6
occ:1.00
OE1 A:GLU17 2.4 17.5 1.0
O A:GLN2 2.4 29.4 1.0
O A:HIS13 2.4 17.1 1.0
OD2 A:ASP16 2.4 18.0 1.0
OD1 A:ASP1 2.6 43.5 1.0
OD2 A:ASP1 2.7 42.2 1.0
ND1 A:HIS13 2.7 22.8 1.0
CG A:ASP1 2.9 42.7 1.0
C A:GLN2 3.4 32.2 1.0
CG A:ASP16 3.5 21.0 1.0
C A:HIS13 3.5 15.6 1.0
CD A:GLU17 3.5 13.1 1.0
CE1 A:HIS13 3.6 23.0 1.0
N A:GLN2 3.7 37.9 1.0
CG A:HIS13 3.7 22.5 1.0
OD1 A:ASP16 3.8 22.5 1.0
CB A:HIS13 4.0 18.8 1.0
CG A:GLU17 4.1 13.7 1.0
CA A:GLN2 4.1 37.0 1.0
NZ A:LYS108 4.3 21.2 1.0
N A:ALA3 4.3 29.6 1.0
CA A:GLY14 4.3 16.6 1.0
N A:GLY14 4.3 15.7 1.0
CB A:ASP1 4.4 40.9 1.0
CA A:HIS13 4.4 17.4 1.0
OE2 A:GLU17 4.5 16.7 1.0
CA A:ALA3 4.5 27.4 1.0
N A:ASP16 4.6 15.5 1.0
C A:ASP1 4.6 39.0 1.0
N A:GLU17 4.7 15.0 1.0
NE2 A:HIS13 4.8 22.6 1.0
CB A:ASP16 4.8 17.3 1.0
C A:ASP16 4.8 16.8 1.0
C A:GLY14 4.8 18.0 1.0
CA A:ASP1 4.8 39.8 1.0
CD2 A:HIS13 4.9 22.0 1.0
CE A:LYS108 4.9 20.1 1.0
N A:GLY15 4.9 15.5 1.0
CB A:GLN2 5.0 42.2 1.0
CA A:ASP16 5.0 16.5 1.0

Reference:

Y.Mezaki, Y.Katsuya, M.Kubota, Y.Matsuura. Crystallization and Structural Analysis of Intact Maltotetraose-Forming Exo-Amylase From Pseudomonas Stutzeri. Biosci.Biotechnol.Biochem. V. 65 222 2001.
ISSN: ISSN 0916-8451
PubMed: 11272837
DOI: 10.1271/BBB.65.222
Page generated: Sat Dec 12 02:57:41 2020

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