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Calcium in PDB 1fo2: Crystal Structure of Human Class I ALPHA1,2-Mannosidase in Complex with 1-Deoxymannojirimycin

Enzymatic activity of Crystal Structure of Human Class I ALPHA1,2-Mannosidase in Complex with 1-Deoxymannojirimycin

All present enzymatic activity of Crystal Structure of Human Class I ALPHA1,2-Mannosidase in Complex with 1-Deoxymannojirimycin:
3.2.1.24;

Protein crystallography data

The structure of Crystal Structure of Human Class I ALPHA1,2-Mannosidase in Complex with 1-Deoxymannojirimycin, PDB code: 1fo2 was solved by F.Vallee, K.Karaveg, K.W.Moremen, A.Herscovics, P.L.Howell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.61 / 2.38
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 96.174, 96.174, 137.118, 90.00, 90.00, 120.00
R / Rfree (%) 19.4 / 24.2

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Human Class I ALPHA1,2-Mannosidase in Complex with 1-Deoxymannojirimycin (pdb code 1fo2). 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 Crystal Structure of Human Class I ALPHA1,2-Mannosidase in Complex with 1-Deoxymannojirimycin, PDB code: 1fo2:

Calcium binding site 1 out of 1 in 1fo2

Go back to Calcium Binding Sites List in 1fo2
Calcium binding site 1 out of 1 in the Crystal Structure of Human Class I ALPHA1,2-Mannosidase in Complex with 1-Deoxymannojirimycin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Human Class I ALPHA1,2-Mannosidase in Complex with 1-Deoxymannojirimycin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca700

b:32.4
occ:1.00
 O A:HOH710 2.6 30.4 1.0
O A:THR688 2.6 23.7 1.0
O3 A:DMJ704 2.7 28.9 1.0
OG1 A:THR688 2.7 25.2 1.0
O A:HOH708 2.7 29.0 1.0
O A:HOH705 2.7 28.0 1.0
O2 A:DMJ704 2.8 26.8 1.0
O A:HOH709 2.8 28.1 1.0
C A:THR688 3.6 24.8 1.0
C2 A:DMJ704 3.6 28.4 1.0
C3 A:DMJ704 3.6 27.9 1.0
CB A:THR688 3.8 25.8 1.0
CA A:THR688 3.9 25.0 1.0
O A:HOH1070 4.0 29.0 1.0
C1 A:DMJ704 4.1 29.4 1.0
OE2 A:GLU467 4.1 30.3 1.0
OE2 A:GLU663 4.2 30.8 1.0
OE2 A:GLU602 4.3 26.9 1.0
CG2 A:THR688 4.4 26.4 1.0
OE1 A:GLU467 4.4 32.2 1.0
O A:HOH1069 4.5 28.6 1.0
OE1 A:GLU599 4.6 25.7 1.0
OE1 A:GLU663 4.6 24.6 1.0
O A:HOH713 4.6 27.0 1.0
CD A:GLU467 4.7 29.6 1.0
N A:GLU689 4.8 26.0 1.0
CD A:GLU663 4.8 26.9 1.0
OE1 A:GLU602 4.8 24.6 1.0

Reference:

F.Vallee, K.Karaveg, A.Herscovics, K.W.Moremen, P.L.Howell. Structural Basis For Catalysis and Inhibition of N-Glycan Processing Class I Alpha 1,2-Mannosidases. J.Biol.Chem. V. 275 41287 2000.
ISSN: ISSN 0021-9258
PubMed: 10995765
DOI: 10.1074/JBC.M006927200
Page generated: Mon Jul 7 14:56:15 2025

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