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Calcium in PDB 5hxm: Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose

Enzymatic activity of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose

All present enzymatic activity of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose:
3.2.1.177;

Protein crystallography data

The structure of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose, PDB code: 5hxm was solved by A.S.Halavaty, S.H.Light, G.Minasov, J.Winsor, S.Grimshaw, L.Shuvalova, S.Peterson, W.F.Anderson, Center For Structural Genomics Of Infectiousdiseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.74 / 1.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 166.157, 102.437, 74.011, 90.00, 103.78, 90.00
R / Rfree (%) 15.2 / 19.5

Other elements in 5hxm:

The structure of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose also contains other interesting chemical elements:

Magnesium (Mg) 5 atoms
Chlorine (Cl) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose (pdb code 5hxm). 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 Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose, PDB code: 5hxm:

Calcium binding site 1 out of 1 in 5hxm

Go back to Calcium Binding Sites List in 5hxm
Calcium binding site 1 out of 1 in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1106

b:39.7
occ:1.00
 OE1 A:GLU939 2.1 37.1 1.0
O A:GLY961 2.3 37.5 1.0
OD1 A:ASP1054 2.3 38.1 1.0
O A:THR958 2.3 38.4 1.0
OE1 A:GLU941 2.5 40.0 1.0
OE2 A:GLU941 2.5 33.8 1.0
O A:ASP1054 2.7 32.7 1.0
CD A:GLU941 2.9 35.5 1.0
CD A:GLU939 3.3 37.1 1.0
C A:THR958 3.4 38.2 1.0
C A:GLY961 3.5 38.4 1.0
CG A:ASP1054 3.5 36.6 1.0
C A:ASP1054 3.5 35.1 1.0
CA A:ASP1054 3.9 35.4 1.0
OE2 A:GLU939 4.0 36.4 1.0
OG1 A:THR958 4.1 35.8 1.0
N A:THR958 4.2 37.7 1.0
N A:GLY961 4.2 40.6 1.0
CB A:GLU939 4.2 36.9 1.0
CG A:GLU939 4.2 36.8 1.0
N A:PHE962 4.3 38.4 1.0
N A:GLY959 4.3 38.8 1.0
CA A:PHE962 4.3 39.5 1.0
CA A:GLY959 4.3 39.1 1.0
CB A:ASP1054 4.4 37.5 1.0
CA A:THR958 4.4 37.6 1.0
OD2 A:ASP1054 4.4 35.5 1.0
CG A:GLU941 4.4 38.6 1.0
CA A:GLY961 4.4 40.2 1.0
CB A:TYR957 4.6 42.8 1.0
CA A:GLU939 4.6 35.9 1.0
N A:HIS1055 4.6 34.0 1.0
C A:GLY959 4.7 39.2 1.0
CB A:PHE962 4.7 37.5 1.0
N A:ALA940 4.7 32.7 1.0
N A:THR960 4.7 40.1 1.0
CB A:HIS1055 4.8 36.1 1.0
CB A:THR958 4.9 37.4 1.0
CD1 A:TYR957 5.0 44.9 1.0

Reference:

S.H.Light, L.A.Cahoon, K.V.Mahasenan, M.Lee, B.Boggess, A.S.Halavaty, S.Mobashery, N.E.Freitag, W.F.Anderson. Transferase Versus Hydrolase: the Role of Conformational Flexibility in Reaction Specificity. Structure V. 25 295 2017.
ISSN: ISSN 1878-4186
PubMed: 28089449
DOI: 10.1016/J.STR.2016.12.007
Page generated: Wed Jul 9 06:36:39 2025

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