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Calcium in PDB 1dl2: Crystal Structure of Class I Alpha-1,2-Mannosidase From Saccharomyces Cerevisiae at 1.54 Angstrom Resolution

Enzymatic activity of Crystal Structure of Class I Alpha-1,2-Mannosidase From Saccharomyces Cerevisiae at 1.54 Angstrom Resolution

All present enzymatic activity of Crystal Structure of Class I Alpha-1,2-Mannosidase From Saccharomyces Cerevisiae at 1.54 Angstrom Resolution:
3.2.1.113;

Protein crystallography data

The structure of Crystal Structure of Class I Alpha-1,2-Mannosidase From Saccharomyces Cerevisiae at 1.54 Angstrom Resolution, PDB code: 1dl2 was solved by F.Vallee, F.Lipari, 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 / 1.54
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 88.397, 88.397, 153.220, 90.00, 90.00, 120.00
R / Rfree (%) 20.9 / 22.7

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Class I Alpha-1,2-Mannosidase From Saccharomyces Cerevisiae at 1.54 Angstrom Resolution (pdb code 1dl2). 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 Class I Alpha-1,2-Mannosidase From Saccharomyces Cerevisiae at 1.54 Angstrom Resolution, PDB code: 1dl2:

Calcium binding site 1 out of 1 in 1dl2

Go back to Calcium Binding Sites List in 1dl2
Calcium binding site 1 out of 1 in the Crystal Structure of Class I Alpha-1,2-Mannosidase From Saccharomyces Cerevisiae at 1.54 Angstrom Resolution


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 Class I Alpha-1,2-Mannosidase From Saccharomyces Cerevisiae at 1.54 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca901

b:25.9
occ:1.00
 O A:HOH1019 2.4 14.3 1.0
O A:HOH951 2.4 18.7 1.0
O A:HOH1088 2.4 15.1 1.0
O A:HOH954 2.5 16.1 1.0
OG1 A:THR525 2.5 14.8 1.0
O A:THR525 2.5 14.2 1.0
O A:HOH1190 3.3 24.6 1.0
C A:THR525 3.4 14.0 1.0
CB A:THR525 3.6 13.3 1.0
CA A:THR525 3.7 13.3 1.0
O A:HOH1189 3.7 11.5 1.0
O2 A:GOL900 3.9 26.7 1.0
OE2 A:GLU279 3.9 14.6 1.0
O A:HOH925 3.9 15.4 1.0
OE2 A:GLU503 4.1 15.9 1.0
OE1 A:GLU279 4.2 15.4 1.0
O A:HOH953 4.2 17.5 1.0
OE1 A:GLU435 4.3 16.1 1.0
O A:HOH1055 4.3 15.5 1.0
OE1 A:GLU438 4.3 18.1 1.0
CG2 A:THR525 4.4 14.8 1.0
CD A:GLU279 4.4 15.7 1.0
N A:GLU526 4.7 12.5 1.0
OE2 A:GLU438 4.7 17.5 1.0
OE1 A:GLU503 4.9 15.6 1.0
CD A:GLU503 4.9 18.3 1.0
CD A:GLU438 5.0 18.2 1.0

Reference:

F.Vallee, F.Lipari, P.Yip, B.Sleno, A.Herscovics, P.L.Howell. Crystal Structure of A Class I ALPHA1,2-Mannosidase Involved in N-Glycan Processing and Endoplasmic Reticulum Quality Control. Embo J. V. 19 581 2000.
ISSN: ISSN 0261-4189
PubMed: 10675327
DOI: 10.1093/EMBOJ/19.4.581
Page generated: Sat Dec 12 02:53:06 2020

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