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Calcium in PDB 4a45: CPGH89CBM32-5, From Clostridium Perfringens, in Complex with Galnac-Beta-1,3-Galactose

Enzymatic activity of CPGH89CBM32-5, From Clostridium Perfringens, in Complex with Galnac-Beta-1,3-Galactose

All present enzymatic activity of CPGH89CBM32-5, From Clostridium Perfringens, in Complex with Galnac-Beta-1,3-Galactose:
3.2.1.50;

Protein crystallography data

The structure of CPGH89CBM32-5, From Clostridium Perfringens, in Complex with Galnac-Beta-1,3-Galactose, PDB code: 4a45 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) 45.13 / 1.75
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 33.803, 58.631, 70.658, 90.00, 90.00, 90.00
R / Rfree (%) 19.855 / 24.571

Other elements in 4a45:

The structure of CPGH89CBM32-5, From Clostridium Perfringens, in Complex with Galnac-Beta-1,3-Galactose also contains other interesting chemical elements:

Sodium (Na) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the CPGH89CBM32-5, From Clostridium Perfringens, in Complex with Galnac-Beta-1,3-Galactose (pdb code 4a45). 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 CPGH89CBM32-5, From Clostridium Perfringens, in Complex with Galnac-Beta-1,3-Galactose, PDB code: 4a45:

Calcium binding site 1 out of 1 in 4a45

Go back to Calcium Binding Sites List in 4a45
Calcium binding site 1 out of 1 in the CPGH89CBM32-5, From Clostridium Perfringens, in Complex with Galnac-Beta-1,3-Galactose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of CPGH89CBM32-5, From Clostridium Perfringens, in Complex with Galnac-Beta-1,3-Galactose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca2496

b:19.9
occ:1.00
 O A:PHE1381 2.4 19.1 1.0
OD1 A:ASP1384 2.4 17.9 1.0
OE2 A:GLU1488 2.5 20.9 1.0
O A:LYS1386 2.5 24.8 1.0
OG1 A:THR1389 2.5 21.8 1.0
O A:THR1389 2.5 21.1 1.0
O A:ALA1487 2.5 18.1 1.0
C A:THR1389 3.4 21.7 1.0
CG A:ASP1384 3.4 20.4 1.0
C A:PHE1381 3.5 19.2 1.0
CD A:GLU1488 3.5 17.0 1.0
C A:LYS1386 3.6 24.3 1.0
C A:ALA1487 3.6 16.6 1.0
CB A:THR1389 3.7 22.5 1.0
OD2 A:ASP1384 3.8 22.3 1.0
CA A:THR1389 3.9 22.1 1.0
N A:LYS1386 4.0 23.0 1.0
CG A:GLU1488 4.0 15.0 1.0
N A:THR1389 4.0 23.1 1.0
CA A:LYS1386 4.2 24.5 1.0
CA A:ALA1487 4.3 16.8 1.0
N A:ILE1390 4.4 21.8 1.0
CA A:PHE1381 4.4 19.8 1.0
CB A:LYS1386 4.4 24.3 1.0
N A:ASP1384 4.4 18.9 1.0
N A:ALA1382 4.5 19.5 1.0
CA A:ALA1382 4.5 18.6 1.0
OE1 A:GLU1488 4.6 18.4 1.0
C A:ALA1382 4.6 18.7 1.0
N A:GLU1387 4.6 24.7 1.0
N A:GLU1488 4.6 15.7 1.0
CB A:PHE1381 4.7 20.0 1.0
CB A:ASP1384 4.7 19.0 1.0
N A:GLY1385 4.8 19.3 1.0
CA A:ILE1390 4.8 21.4 1.0
CA A:GLU1387 4.8 26.0 1.0
CG2 A:THR1389 4.8 22.1 1.0
CA A:GLU1488 4.8 15.6 1.0
CB A:ALA1487 4.8 15.9 1.0
N A:ILE1383 4.9 18.3 1.0
CA A:ASP1384 4.9 19.7 1.0
C A:GLU1387 4.9 25.6 1.0
O A:ALA1382 4.9 18.2 1.0
CB A:GLU1488 5.0 15.6 1.0

Reference:

E.Ficko-Blean, C.P.Stuart, M.D.Suits, M.Cid, M.Tessier, R.J.Woods, A.B.Boraston. Carbohydrate Recognition By An Architecturally Complex Alpha-N-Acetylglucosaminidase From Clostridium Perfringens. Plos One V. 7 33524 2012.
ISSN: ISSN 1932-6203
PubMed: 22479408
DOI: 10.1371/JOURNAL.PONE.0033524
Page generated: Sat Jul 13 21:55:00 2024

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