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Calcium in PDB 1kkt: 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: 1kkt 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 (%) 19.3 / 23.9

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 1kkt). 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: 1kkt:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1kkt

Go back to Calcium Binding Sites List in 1kkt
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:18.0
occ:1.00
 O A:THR501 2.4 14.2 1.0
OG1 A:THR501 2.5 16.8 1.0
O A:HOH930 2.5 17.3 1.0
O A:HOH926 2.5 16.1 1.0
O A:HOH927 2.5 17.8 1.0
O A:HOH929 2.6 14.0 1.0
O A:HOH928 2.6 15.0 1.0
O A:HOH933 2.9 19.9 1.0
C A:THR501 3.4 16.1 1.0
CB A:THR501 3.6 14.5 1.0
CA A:THR501 3.8 14.2 1.0
OE1 A:GLU271 4.1 15.4 1.0
O A:HOH936 4.2 12.8 1.0
OE2 A:GLU472 4.2 14.5 1.0
CG2 A:THR501 4.2 12.4 1.0
OE2 A:GLU412 4.4 17.2 1.0
O A:HOH935 4.5 28.7 1.0
O A:HOH931 4.5 14.6 1.0
OE2 A:GLU271 4.6 11.3 1.0
OE1 A:GLU472 4.6 11.6 1.0
OE1 A:GLU409 4.6 15.1 1.0
O A:HOH832 4.6 22.0 1.0
N A:GLU502 4.7 14.4 1.0
CD A:GLU271 4.8 13.4 1.0
CD A:GLU472 4.8 15.7 1.0

Calcium binding site 2 out of 2 in 1kkt

Go back to Calcium Binding Sites List in 1kkt
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:27.1
occ:1.00
 O B:THR501 2.4 24.4 1.0
O B:HOH838 2.4 33.7 1.0
O B:HOH837 2.5 28.2 1.0
O B:HOH836 2.5 21.1 1.0
OG1 B:THR501 2.6 24.3 1.0
O B:HOH835 2.7 21.3 1.0
O B:HOH844 2.9 38.7 1.0
C B:THR501 3.4 25.6 1.0
CB B:THR501 3.7 25.5 1.0
CA B:THR501 3.8 26.3 1.0
O B:HOH840 4.0 24.5 1.0
OE1 B:GLU271 4.1 28.3 1.0
OE2 B:GLU472 4.2 22.5 1.0
CG2 B:THR501 4.3 25.8 1.0
O B:HOH839 4.4 25.0 1.0
OE2 B:GLU412 4.5 30.9 1.0
OE1 B:GLU472 4.6 25.0 1.0
N B:GLU502 4.6 24.2 1.0
OE2 B:GLU271 4.7 27.1 1.0
OE1 B:GLU409 4.7 27.0 1.0
CD B:GLU271 4.8 29.0 1.0
CD B:GLU472 4.8 24.5 1.0
O B:HOH842 4.9 40.6 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 11:25:06 2024

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