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Calcium in PDB 1g6i: Crystal Structure of the Yeast Alpha-1,2-Mannosidase with Bound 1- Deoxymannojirimycin at 1.59 A Resolution

Enzymatic activity of Crystal Structure of the Yeast Alpha-1,2-Mannosidase with Bound 1- Deoxymannojirimycin at 1.59 A Resolution

All present enzymatic activity of Crystal Structure of the Yeast Alpha-1,2-Mannosidase with Bound 1- Deoxymannojirimycin at 1.59 A Resolution:
3.2.1.113;

Protein crystallography data

The structure of Crystal Structure of the Yeast Alpha-1,2-Mannosidase with Bound 1- Deoxymannojirimycin at 1.59 A Resolution, PDB code: 1g6i was solved by A.Herscovics, F.Lipari, B.Sleno, P.A.Romera, F.Vallee, P.Yip, P.A.Howell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.56 / 1.59
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 89.052, 89.052, 153.142, 90.00, 90.00, 120.00
R / Rfree (%) 23 / 25.3

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Yeast Alpha-1,2-Mannosidase with Bound 1- Deoxymannojirimycin at 1.59 A Resolution (pdb code 1g6i). 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 the Yeast Alpha-1,2-Mannosidase with Bound 1- Deoxymannojirimycin at 1.59 A Resolution, PDB code: 1g6i:

Calcium binding site 1 out of 1 in 1g6i

Go back to Calcium Binding Sites List in 1g6i
Calcium binding site 1 out of 1 in the Crystal Structure of the Yeast Alpha-1,2-Mannosidase with Bound 1- Deoxymannojirimycin at 1.59 A 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 the Yeast Alpha-1,2-Mannosidase with Bound 1- Deoxymannojirimycin at 1.59 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1001

b:18.8
occ:1.00
 O A:HOH1392 2.5 18.6 1.0
O A:HOH1323 2.6 16.8 1.0
OG1 A:THR525 2.6 15.6 1.0
O2 A:DMJ1002 2.6 27.6 1.0
O A:THR525 2.6 14.8 1.0
O3 A:DMJ1002 2.8 26.9 1.0
C A:THR525 3.6 15.3 1.0
C2 A:DMJ1002 3.6 27.2 1.0
C3 A:DMJ1002 3.6 27.0 1.0
CB A:THR525 3.7 15.4 1.0
CA A:THR525 3.9 15.9 1.0
OE2 A:GLU279 4.0 16.7 1.0
O A:HOH1229 4.1 16.8 1.0
C1 A:DMJ1002 4.2 26.1 1.0
OE2 A:GLU503 4.2 17.5 1.0
OE1 A:GLU279 4.3 16.1 1.0
OE1 A:GLU438 4.3 18.8 1.0
O A:HOH1359 4.4 16.0 1.0
CG2 A:THR525 4.4 15.3 1.0
OE1 A:GLU435 4.4 20.0 1.0
O A:HOH1257 4.5 20.1 1.0
CD A:GLU279 4.6 17.7 1.0
OE2 A:GLU438 4.7 18.1 1.0
OE1 A:GLU503 4.8 18.1 1.0
O A:HOH1255 4.8 60.6 1.0
N A:GLU526 4.8 14.6 1.0
CD A:GLU438 4.9 19.8 1.0
CD A:GLU503 4.9 18.1 1.0

Reference:

A.Herscovics, F.Lipari, B.Sleno, P.A.Romera, F.Vallee, P.Yip, P.A.Howell. Structure and Function of Class I A1,2-Mannosidases Involved in Glycoprotein Biosynthesis. Carbohydrate Bioengineering. 28 2002INTERDISCIPLINARYAPPROACHES..
Page generated: Mon Jul 7 15:07:44 2025

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