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Calcium in PDB 4a4a: CPGH89 (E483Q, E601Q), From Clostridium Perfringens, in Complex with Its Substrate Glcnac-Alpha-1,4-Galactose

Enzymatic activity of CPGH89 (E483Q, E601Q), From Clostridium Perfringens, in Complex with Its Substrate Glcnac-Alpha-1,4-Galactose

All present enzymatic activity of CPGH89 (E483Q, E601Q), From Clostridium Perfringens, in Complex with Its Substrate Glcnac-Alpha-1,4-Galactose:
3.2.1.50;

Protein crystallography data

The structure of CPGH89 (E483Q, E601Q), From Clostridium Perfringens, in Complex with Its Substrate Glcnac-Alpha-1,4-Galactose, PDB code: 4a4a was solved by E.Ficko-Blean, C.P.Stuart, M.D.Suits, M.Cid, M.Tessier, R.J.Woods, A.B.Boraston, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 78.81 / 1.90
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 90.996, 90.996, 252.856, 90.00, 90.00, 120.00
R / Rfree (%) 16.9 / 21

Calcium Binding Sites:

The binding sites of Calcium atom in the CPGH89 (E483Q, E601Q), From Clostridium Perfringens, in Complex with Its Substrate Glcnac-Alpha-1,4-Galactose (pdb code 4a4a). 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 CPGH89 (E483Q, E601Q), From Clostridium Perfringens, in Complex with Its Substrate Glcnac-Alpha-1,4-Galactose, PDB code: 4a4a:

Calcium binding site 1 out of 1 in 4a4a

Go back to Calcium Binding Sites List in 4a4a
Calcium binding site 1 out of 1 in the CPGH89 (E483Q, E601Q), From Clostridium Perfringens, in Complex with Its Substrate Glcnac-Alpha-1,4-Galactose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of CPGH89 (E483Q, E601Q), From Clostridium Perfringens, in Complex with Its Substrate Glcnac-Alpha-1,4-Galactose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1925

b:24.8
occ:1.00
 O A:LEU48 2.3 24.0 1.0
OE2 A:GLU149 2.3 25.4 1.0
O A:ASP53 2.4 26.6 1.0
OD1 A:ASP51 2.4 24.6 1.0
O A:ALA148 2.4 22.6 1.0
O A:THR56 2.5 21.9 1.0
OG1 A:THR56 2.5 21.1 1.0
C A:THR56 3.3 22.9 1.0
CG A:ASP51 3.4 27.3 1.0
CD A:GLU149 3.4 20.3 1.0
C A:LEU48 3.5 23.7 1.0
C A:ASP53 3.5 26.6 1.0
C A:ALA148 3.6 22.6 1.0
CB A:THR56 3.7 22.5 1.0
OD2 A:ASP51 3.8 25.8 1.0
CA A:THR56 3.9 22.8 1.0
CG A:GLU149 4.0 23.0 1.0
N A:ASP53 4.0 25.9 1.0
N A:THR56 4.0 24.8 1.0
CA A:ASP53 4.1 26.1 1.0
N A:TYR57 4.2 22.2 1.0
CB A:ASP53 4.3 24.2 1.0
CA A:LEU48 4.3 23.3 1.0
N A:ASP51 4.4 24.8 1.0
CA A:ALA148 4.4 22.1 1.0
N A:ALA49 4.4 23.1 1.0
CA A:ALA49 4.5 23.3 1.0
C A:ALA49 4.5 23.5 1.0
OE1 A:GLU149 4.5 22.1 1.0
CA A:TYR57 4.5 21.8 1.0
N A:GLU149 4.6 21.4 1.0
N A:LEU54 4.6 26.0 1.0
CB A:ASP51 4.6 24.9 1.0
CB A:LEU48 4.6 24.7 1.0
CA A:GLU149 4.7 22.2 1.0
N A:ILE50 4.8 22.4 1.0
CA A:LEU54 4.8 27.3 1.0
CA A:ASP51 4.8 25.7 1.0
O A:ALA49 4.9 24.1 1.0
N A:GLY52 4.9 25.9 1.0
CB A:GLU149 4.9 21.6 1.0
CG2 A:THR56 5.0 23.4 1.0
C A:LEU54 5.0 27.3 1.0
C A:ASP51 5.0 26.3 1.0

Reference:

E.Ficko-Blean, A.B.Boraston. Structural Analysis of A Bacterial Exo-Alpha-D-N-Acetylglucosaminidase in Complex with An Unusual Disaccharide Found in Class III Mucin. Glycobiology V. 22 590 2012.
ISSN: ESSN 1460-2423
PubMed: 22090394
DOI: 10.1093/GLYCOB/CWR165
Page generated: Sat Jul 13 21:55:00 2024

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