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Calcium in PDB 1krf: Structure of P. Citrinum Alpha 1,2-Mannosidase Reveals the Basis For Differences in Specificity of the Er and Golgi Class I Enzymes

Enzymatic activity of Structure of P. Citrinum Alpha 1,2-Mannosidase Reveals the Basis For Differences in Specificity of the Er and Golgi Class I Enzymes

All present enzymatic activity of Structure of P. Citrinum Alpha 1,2-Mannosidase Reveals the Basis For Differences in Specificity of the Er and Golgi Class I Enzymes:
3.2.1.113;

Protein crystallography data

The structure of Structure of P. Citrinum Alpha 1,2-Mannosidase Reveals the Basis For Differences in Specificity of the Er and Golgi Class I Enzymes, PDB code: 1krf was solved by Y.D.Lobsanov, F.Vallee, A.Imberty, T.Yoshida, P.Yip, A.Herscovics, P.L.Howell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 56.487, 110.997, 86.235, 90.00, 99.17, 90.00
R / Rfree (%) 19.9 / 23.6

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of P. Citrinum Alpha 1,2-Mannosidase Reveals the Basis For Differences in Specificity of the Er and Golgi Class I Enzymes (pdb code 1krf). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of P. Citrinum Alpha 1,2-Mannosidase Reveals the Basis For Differences in Specificity of the Er and Golgi Class I Enzymes, PDB code: 1krf:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1krf

Go back to Calcium Binding Sites List in 1krf
Calcium binding site 1 out of 2 in the Structure of P. Citrinum Alpha 1,2-Mannosidase Reveals the Basis For Differences in Specificity of the Er and Golgi Class I Enzymes


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of P. Citrinum Alpha 1,2-Mannosidase Reveals the Basis For Differences in Specificity of the Er and Golgi Class I Enzymes within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca550

b:18.6
occ:1.00
 OG1 A:THR501 2.6 15.2 1.0
O A:THR501 2.6 11.6 1.0
O2 A:KIF901 2.6 14.5 1.0
O A:HOH1028 2.6 13.8 1.0
O A:HOH1026 2.7 13.5 1.0
O A:HOH1027 2.7 15.4 1.0
O A:HOH1029 2.7 11.0 1.0
O3 A:KIF901 2.7 13.7 1.0
C A:THR501 3.5 15.1 1.0
C3 A:KIF901 3.5 13.9 1.0
C2 A:KIF901 3.6 16.9 1.0
CB A:THR501 3.7 14.6 1.0
CA A:THR501 3.8 14.0 1.0
OE1 A:GLU271 4.0 13.6 1.0
O A:HOH1031 4.1 11.2 1.0
OE2 A:GLU472 4.3 10.2 1.0
C1 A:KIF901 4.3 15.2 1.0
CG2 A:THR501 4.4 11.2 1.0
OE2 A:GLU412 4.4 14.4 1.0
O A:HOH1030 4.5 15.8 1.0
OE1 A:GLU472 4.6 11.5 1.0
OE2 A:GLU271 4.6 10.5 1.0
CD A:GLU271 4.7 13.2 1.0
OE1 A:GLU409 4.7 15.1 1.0
N A:GLU502 4.7 13.5 1.0
O A:HOH932 4.8 20.4 1.0
CD A:GLU472 4.9 12.3 1.0
N9 A:KIF901 5.0 20.3 1.0
OE1 A:GLU412 5.0 14.0 1.0

Calcium binding site 2 out of 2 in 1krf

Go back to Calcium Binding Sites List in 1krf
Calcium binding site 2 out of 2 in the Structure of P. Citrinum Alpha 1,2-Mannosidase Reveals the Basis For Differences in Specificity of the Er and Golgi Class I Enzymes


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of P. Citrinum Alpha 1,2-Mannosidase Reveals the Basis For Differences in Specificity of the Er and Golgi Class I Enzymes within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca551

b:28.1
occ:1.00
 O B:THR501 2.6 22.0 1.0
O B:HOH937 2.6 22.5 1.0
OG1 B:THR501 2.7 21.0 1.0
O2 B:KIF902 2.7 24.9 1.0
O B:HOH938 2.7 19.4 1.0
O B:HOH936 2.7 16.1 1.0
O B:HOH958 2.8 29.9 1.0
O3 B:KIF902 2.8 24.8 1.0
C B:THR501 3.6 23.4 1.0
C3 B:KIF902 3.6 23.1 1.0
C2 B:KIF902 3.7 25.7 1.0
CB B:THR501 3.7 23.6 1.0
CA B:THR501 3.9 23.6 1.0
OE1 B:GLU271 4.0 26.0 1.0
O B:HOH940 4.0 20.6 1.0
OE2 B:GLU472 4.2 21.4 1.0
OE2 B:GLU412 4.3 26.9 1.0
C1 B:KIF902 4.4 25.4 1.0
CG2 B:THR501 4.4 23.7 1.0
O B:HOH939 4.5 22.1 1.0
OE2 B:GLU271 4.6 25.2 1.0
CD B:GLU271 4.7 25.6 1.0
OE1 B:GLU472 4.7 21.4 1.0
O B:HOH954 4.8 28.8 1.0
N B:GLU502 4.8 21.8 1.0
OE1 B:GLU409 4.8 22.9 1.0
CD B:GLU472 4.9 22.1 1.0
OE1 B:GLU412 4.9 27.5 1.0

Reference:

Y.D.Lobsanov, F.Vallee, A.Imberty, T.Yoshida, P.Yip, A.Herscovics, P.L.Howell. Structure of Penicillium Citrinum Alpha 1,2-Mannosidase Reveals the Basis For Differences in Specificity of the Endoplasmic Reticulum and Golgi Class I Enzymes. J.Biol.Chem. V. 277 5620 2002.
ISSN: ISSN 0021-9258
PubMed: 11714724
DOI: 10.1074/JBC.M110243200
Page generated: Thu Jul 11 11:29:02 2024

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