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Calcium in PDB 1kck: Bacillus Circulans Strain 251 Cyclodextrin Glycosyl Transferase Mutant N193G

Enzymatic activity of Bacillus Circulans Strain 251 Cyclodextrin Glycosyl Transferase Mutant N193G

All present enzymatic activity of Bacillus Circulans Strain 251 Cyclodextrin Glycosyl Transferase Mutant N193G:
2.4.1.19;

Protein crystallography data

The structure of Bacillus Circulans Strain 251 Cyclodextrin Glycosyl Transferase Mutant N193G, PDB code: 1kck was solved by H.J.Rozeboom, J.C.M.Uitdehaag, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.64 / 2.43
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 120.686, 111.162, 65.944, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / 20.5

Calcium Binding Sites:

The binding sites of Calcium atom in the Bacillus Circulans Strain 251 Cyclodextrin Glycosyl Transferase Mutant N193G (pdb code 1kck). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Bacillus Circulans Strain 251 Cyclodextrin Glycosyl Transferase Mutant N193G, PDB code: 1kck:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1kck

Go back to Calcium Binding Sites List in 1kck
Calcium binding site 1 out of 2 in the Bacillus Circulans Strain 251 Cyclodextrin Glycosyl Transferase Mutant N193G


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Bacillus Circulans Strain 251 Cyclodextrin Glycosyl Transferase Mutant N193G within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca690

b:24.1
occ:1.00
OD1 A:ASN33 2.2 34.3 1.0
OD2 A:ASP53 2.3 20.8 1.0
OD1 A:ASN32 2.4 26.5 1.0
O A:HOH740 2.5 17.9 1.0
O A:ASN29 2.6 29.8 1.0
O A:GLY51 2.6 23.8 1.0
OD1 A:ASP27 2.8 22.3 1.0
CG A:ASN33 3.3 30.4 1.0
CG A:ASP53 3.4 20.7 1.0
C A:ASN29 3.5 29.1 1.0
CG A:ASP27 3.5 23.6 1.0
CG A:ASN32 3.5 27.3 1.0
C A:GLY51 3.7 22.8 1.0
OD2 A:ASP27 3.8 24.2 1.0
CB A:ASP53 3.9 21.3 1.0
ND2 A:ASN33 4.0 31.4 1.0
N A:ASN33 4.0 26.6 1.0
ND2 A:ASN32 4.1 24.8 1.0
CA A:GLY51 4.1 22.9 1.0
N A:PRO30 4.2 30.6 1.0
CA A:PRO30 4.2 30.5 1.0
O A:ALA111 4.2 20.6 1.0
CA A:ASN33 4.3 28.4 1.0
N A:ASN29 4.3 26.0 1.0
C A:ASN32 4.4 25.9 1.0
CB A:ASN33 4.4 29.0 1.0
CA A:ASN29 4.4 27.6 1.0
OD1 A:ASP53 4.5 23.9 1.0
CB A:ASP27 4.6 22.9 1.0
C A:PRO30 4.7 31.2 1.0
N A:ASN32 4.7 30.1 1.0
CA A:ASP27 4.7 22.3 1.0
CB A:ASN32 4.7 27.0 1.0
C A:GLY52 4.7 20.0 1.0
N A:ASP53 4.8 19.2 1.0
CA A:ASN32 4.8 27.0 1.0
CB A:ASN29 4.8 28.7 1.0
N A:GLY52 4.8 22.6 1.0
O A:GLY52 4.9 19.8 1.0
O A:ASN32 4.9 26.1 1.0
CA A:ASP53 5.0 20.5 1.0

Calcium binding site 2 out of 2 in 1kck

Go back to Calcium Binding Sites List in 1kck
Calcium binding site 2 out of 2 in the Bacillus Circulans Strain 251 Cyclodextrin Glycosyl Transferase Mutant N193G


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Bacillus Circulans Strain 251 Cyclodextrin Glycosyl Transferase Mutant N193G within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca691

b:17.9
occ:1.00
O A:HIS233 2.4 16.0 1.0
OD1 A:ASN139 2.5 14.6 1.0
O A:HOH729 2.5 11.5 1.0
O A:HOH717 2.5 11.4 1.0
OD1 A:ASP199 2.5 19.2 1.0
O A:HOH708 2.6 9.5 1.0
OD2 A:ASP199 2.6 20.5 1.0
O A:ILE190 2.7 14.7 1.0
CG A:ASP199 2.9 20.2 1.0
CG A:ASN139 3.6 13.7 1.0
C A:HIS233 3.6 14.6 1.0
C A:ILE190 3.8 16.0 1.0
ND2 A:ASN139 4.2 13.7 1.0
CB A:HIS233 4.3 14.2 1.0
O A:ASN139 4.3 21.1 1.0
CA A:ILE190 4.4 15.9 1.0
CB A:ASP199 4.4 18.3 1.0
N A:MET234 4.5 14.8 1.0
CA A:MET234 4.5 14.4 1.0
CA A:HIS233 4.5 14.0 1.0
O A:GLY189 4.6 17.0 1.0
O A:HOH748 4.6 19.5 1.0
CG A:MET234 4.7 15.1 1.0
O A:LYS192 4.7 17.7 1.0
O A:LEU200 4.8 15.7 1.0
CB A:ASN139 4.8 16.2 1.0
ND1 A:HIS176 4.8 21.0 1.0
O A:HOH787 4.9 17.3 1.0
N A:TYR191 4.9 15.8 1.0
CG2 A:ILE190 5.0 14.1 1.0

Reference:

H.Leemhuis, J.C.Uitdehaag, H.J.Rozeboom, B.W.Dijkstra, L.Dijkhuizen. The Remote Substrate Binding Subsite -6 in Cyclodextrin-Glycosyltransferase Controls the Transferase Activity of the Enzyme Via An Induced-Fit Mechanism. J.Biol.Chem. V. 277 1113 2002.
ISSN: ISSN 0021-9258
PubMed: 11696539
DOI: 10.1074/JBC.M106667200
Page generated: Thu Jul 11 11:20:12 2024

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