Calcium in PDB 6a0j: Cyclic Alpha-Maltosyl-(1-->6)-Maltose Hydrolase From Arthrobacter Globiformis, Complex with Cyclic Alpha-Maltosyl-(1-->6)-Maltose

Protein crystallography data

The structure of Cyclic Alpha-Maltosyl-(1-->6)-Maltose Hydrolase From Arthrobacter Globiformis, Complex with Cyclic Alpha-Maltosyl-(1-->6)-Maltose, PDB code: 6a0j was solved by M.Kohno, T.Arakawa, T.Mori, T.Nishimoto, S.Fushinobu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 68.67 / 1.60
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 72.703, 72.703, 209.185, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 19

Calcium Binding Sites:

The binding sites of Calcium atom in the Cyclic Alpha-Maltosyl-(1-->6)-Maltose Hydrolase From Arthrobacter Globiformis, Complex with Cyclic Alpha-Maltosyl-(1-->6)-Maltose (pdb code 6a0j). 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 Cyclic Alpha-Maltosyl-(1-->6)-Maltose Hydrolase From Arthrobacter Globiformis, Complex with Cyclic Alpha-Maltosyl-(1-->6)-Maltose, PDB code: 6a0j:

Calcium binding site 1 out of 1 in 6a0j

Go back to Calcium Binding Sites List in 6a0j
Calcium binding site 1 out of 1 in the Cyclic Alpha-Maltosyl-(1-->6)-Maltose Hydrolase From Arthrobacter Globiformis, Complex with Cyclic Alpha-Maltosyl-(1-->6)-Maltose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Cyclic Alpha-Maltosyl-(1-->6)-Maltose Hydrolase From Arthrobacter Globiformis, Complex with Cyclic Alpha-Maltosyl-(1-->6)-Maltose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca505

b:15.5
occ:1.00
OD2 A:ASP48 2.6 11.1 1.0
OD1 A:ASP28 2.7 14.4 1.0
O A:ASP24 2.7 13.2 1.0
O A:GLY46 2.7 12.3 1.0
OD1 A:ASN22 2.7 13.0 1.0
O A:HOH775 2.8 15.4 1.0
CG A:ASN22 3.3 13.4 1.0
ND2 A:ASN22 3.5 14.2 1.0
C A:ASP24 3.7 15.8 1.0
CG A:ASP48 3.7 11.3 1.0
C A:GLY46 3.7 10.8 1.0
N A:ASP28 3.8 13.2 1.0
CG A:ASP28 3.8 15.7 1.0
CB A:LEU27 3.9 12.2 1.0
CA A:GLY46 4.0 10.9 1.0
C A:LEU27 4.1 14.3 1.0
CB A:ASP48 4.1 10.5 1.0
N A:ASP24 4.1 14.4 1.0
CA A:ASP28 4.2 14.3 1.0
CA A:ASP24 4.4 13.8 1.0
CA A:LEU27 4.4 14.5 1.0
CB A:ASN22 4.4 13.3 1.0
N A:PRO25 4.5 16.3 1.0
CA A:PRO25 4.6 19.1 1.0
O A:LEU27 4.6 12.9 1.0
N A:LEU27 4.6 15.9 1.0
CB A:ASP28 4.6 13.9 1.0
CA A:ASN22 4.6 14.3 1.0
O A:ARG92 4.7 13.6 1.0
OD1 A:ASP48 4.7 10.3 1.0
O A:HOH700 4.7 31.9 1.0
OD2 A:ASP28 4.7 18.2 1.0
CB A:ASP24 4.8 13.6 1.0
N A:ALA23 4.8 12.3 1.0
CG A:LEU27 4.9 12.8 1.0
N A:GLY47 4.9 10.4 1.0
C A:ASN22 4.9 15.5 1.0
C A:GLY47 4.9 10.9 1.0
O A:GLY47 4.9 12.2 1.0
C A:PRO25 4.9 18.3 1.0

Reference:

M.Kohno, T.Arakawa, H.Ota, T.Mori, T.Nishimoto, S.Fushinobu. Structural Features of A Bacterial Cyclic Alpha-Maltosyl-(1→6)-Maltose (Cmm) Hydrolase Critical For Cmm Recognition and Hydrolysis. J. Biol. Chem. V. 293 16874 2018.
ISSN: ESSN 1083-351X
PubMed: 30181215
DOI: 10.1074/JBC.RA118.004472
Page generated: Sat Dec 12 05:56:20 2020

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