Calcium in PDB 1kre: 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: 1kre 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 / R_free (%)*	19.8 / 24.3

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

Calcium binding site 1 out of 2 in 1kre

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Calcium Binding Sites List in 1kre

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:17.3 occ:1.00	OG1	A:THR501	2.6	12.0	1.0
	O	A:HOH1028	2.6	13.2	1.0
	O	A:THR501	2.6	9.2	1.0
	O	A:HOH1026	2.7	14.8	1.0
	O	A:HOH1027	2.7	19.5	1.0
	O	A:HOH1029	2.7	13.4	1.0
	O2	A:DMJ901	2.8	27.2	1.0
	O3	A:DMJ901	2.9	24.7	1.0
	C	A:THR501	3.6	12.5	1.0
	CB	A:THR501	3.7	11.1	1.0
	C2	A:DMJ901	3.8	28.1	1.0
	C3	A:DMJ901	3.8	26.2	1.0
	CA	A:THR501	3.9	11.7	1.0
	OE1	A:GLU271	4.0	10.7	1.0
	O	A:HOH1031	4.1	9.7	1.0
	OE2	A:GLU472	4.2	10.9	1.0
	O	A:HOH1030	4.3	13.8	1.0
	OE2	A:GLU412	4.3	13.8	1.0
	C1	A:DMJ901	4.4	26.3	1.0
	CG2	A:THR501	4.5	8.3	1.0
	OE2	A:GLU271	4.5	9.2	1.0
	O	A:HOH932	4.5	29.9	1.0
	OE1	A:GLU409	4.6	14.8	1.0
	CD	A:GLU271	4.6	9.4	1.0
	OE1	A:GLU472	4.8	8.7	1.0
	N	A:GLU502	4.8	11.2	1.0
	OG	A:SER268	4.9	26.4	1.0
	CD	A:GLU472	4.9	11.4	1.0
	CG	A:GLU409	5.0	10.7	1.0

Calcium binding site 2 out of 2 in 1kre

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Calcium Binding Sites List in 1kre

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:28.8 occ:1.00	O	B:HOH937	2.6	23.9	1.0
	O	B:THR501	2.7	20.6	1.0
	O	B:HOH936	2.7	15.9	1.0
	O	B:HOH959	2.7	35.1	1.0
	OG1	B:THR501	2.8	20.9	1.0
	O	B:HOH938	2.8	28.8	1.0
	O2	B:DMJ902	2.9	46.0	1.0
	O3	B:DMJ902	2.9	43.5	1.0
	C	B:THR501	3.6	22.2	1.0
	C2	B:DMJ902	3.8	44.7	1.0
	C3	B:DMJ902	3.8	43.1	1.0
	CB	B:THR501	3.8	22.0	1.0
	OE1	B:GLU271	3.9	21.9	1.0
	CA	B:THR501	3.9	22.8	1.0
	O	B:HOH940	3.9	19.3	1.0
	OE2	B:GLU472	4.2	21.3	1.0
	OE2	B:GLU412	4.3	28.4	1.0
	O	B:HOH939	4.4	21.7	1.0
	C1	B:DMJ902	4.4	43.2	1.0
	CG2	B:THR501	4.5	22.3	1.0
	O	B:HOH955	4.6	35.2	1.0
	OE2	B:GLU271	4.6	18.0	1.0
	CD	B:GLU271	4.7	20.5	1.0
	OE1	B:GLU409	4.8	23.4	1.0
	N	B:GLU502	4.9	20.4	1.0
	OE1	B:GLU472	4.9	22.1	1.0
	CD	B:GLU472	5.0	20.6	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 11:26:56 2024

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