Atomistry » Calcium » PDB 5z4p-5zxg » 5zxg
Atomistry »
  Calcium »
    PDB 5z4p-5zxg »
      5zxg »

Calcium in PDB 5zxg: Cyclic Alpha-Maltosyl-(1-->6)-Maltose Hydrolase From Arthrobacter Globiformis, Ligand-Free Form

Protein crystallography data

The structure of Cyclic Alpha-Maltosyl-(1-->6)-Maltose Hydrolase From Arthrobacter Globiformis, Ligand-Free Form, PDB code: 5zxg 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) 89.90 / 2.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 48.250, 179.798, 63.412, 90.00, 113.61, 90.00
R / Rfree (%) 18.8 / 24.8

Calcium Binding Sites:

The binding sites of Calcium atom in the Cyclic Alpha-Maltosyl-(1-->6)-Maltose Hydrolase From Arthrobacter Globiformis, Ligand-Free Form (pdb code 5zxg). 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, Ligand-Free Form, PDB code: 5zxg:

Calcium binding site 1 out of 1 in 5zxg

Go back to Calcium Binding Sites List in 5zxg
Calcium binding site 1 out of 1 in the Cyclic Alpha-Maltosyl-(1-->6)-Maltose Hydrolase From Arthrobacter Globiformis, Ligand-Free Form


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, Ligand-Free Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca501

b:41.0
occ:1.00
O A:GLY47 2.4 20.3 1.0
OD2 A:ASP49 2.5 20.8 1.0
OD1 A:ASP29 2.6 29.0 1.0
OD1 A:ASN23 2.6 27.7 1.0
O A:ASP25 2.7 30.7 1.0
O A:HOH685 2.8 29.0 1.0
CG A:ASN23 3.3 29.9 1.0
CG A:ASP49 3.5 22.8 1.0
C A:GLY47 3.5 18.8 1.0
C A:ASP25 3.5 33.7 1.0
CG A:ASP29 3.7 34.7 1.0
ND2 A:ASN23 3.8 29.9 1.0
CB A:ASP49 3.9 23.2 1.0
CA A:GLY47 3.9 19.1 1.0
N A:ASP25 4.0 30.6 1.0
CB A:LEU28 4.0 27.7 1.0
N A:ASP29 4.2 31.1 1.0
CA A:ASP25 4.2 31.1 1.0
CB A:ASN23 4.3 28.4 1.0
CA A:ASN23 4.3 26.6 1.0
N A:PRO26 4.4 41.0 1.0
OD2 A:ASP29 4.4 34.8 1.0
CA A:ASP29 4.4 33.7 1.0
C A:LEU28 4.5 30.4 1.0
OD1 A:ASP49 4.5 23.8 1.0
CA A:PRO26 4.6 41.3 1.0
CB A:ASP25 4.6 32.4 1.0
O A:GLY48 4.6 18.8 1.0
C A:GLY48 4.6 19.0 1.0
CA A:LEU28 4.6 29.1 1.0
O A:ARG93 4.7 21.1 1.0
N A:GLY48 4.7 17.8 1.0
CB A:ASP29 4.7 35.0 1.0
C A:ASN23 4.7 27.6 1.0
N A:ALA24 4.7 27.7 1.0
N A:LEU28 4.8 30.4 1.0
N A:ASP49 4.8 20.1 1.0
CG A:LEU28 4.9 30.3 1.0
CD1 A:LEU28 4.9 30.4 1.0
CA A:ASP49 4.9 23.4 1.0
O A:HOH728 4.9 27.6 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: Mon Jul 15 15:55:40 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy