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Magnesium in PDB 1bvw: Cellobiohydrolase II (CEL6A) From Humicola Insolens

Enzymatic activity of Cellobiohydrolase II (CEL6A) From Humicola Insolens

All present enzymatic activity of Cellobiohydrolase II (CEL6A) From Humicola Insolens:
3.2.1.91;

Protein crystallography data

The structure of Cellobiohydrolase II (CEL6A) From Humicola Insolens, PDB code: 1bvw was solved by A.Varrot, G.J.Davies, M.Schulein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.92
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.510, 68.100, 53.710, 90.00, 110.93, 90.00
R / Rfree (%) 14.2 / 21

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cellobiohydrolase II (CEL6A) From Humicola Insolens (pdb code 1bvw). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Cellobiohydrolase II (CEL6A) From Humicola Insolens, PDB code: 1bvw:

Magnesium binding site 1 out of 1 in 1bvw

Go back to Magnesium Binding Sites List in 1bvw
Magnesium binding site 1 out of 1 in the Cellobiohydrolase II (CEL6A) From Humicola Insolens


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cellobiohydrolase II (CEL6A) From Humicola Insolens within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg550

b:32.8
occ:1.00
O A:HOH1055 1.8 30.1 1.0
O A:HOH952 2.1 23.1 1.0
O A:HOH993 2.2 26.2 1.0
O A:HOH959 2.2 24.0 1.0
O A:HOH947 2.2 23.1 1.0
O A:HOH1147 2.4 37.4 1.0
OE2 A:GLU336 3.9 14.0 1.0
OE1 A:GLU336 4.3 15.3 1.0
NZ A:LYS332 4.3 20.2 1.0
O A:HOH1013 4.4 27.9 1.0
CE A:LYS332 4.4 18.4 1.0
CD A:GLU336 4.5 14.7 1.0
O A:HOH1138 5.0 36.3 1.0

Reference:

A.Varrot, S.Hastrup, M.Schulein, G.J.Davies. Crystal Structure of the Catalytic Core Domain of the Family 6 Cellobiohydrolase II, CEL6A, From Humicola Insolens, at 1.92 A Resolution. Biochem.J. V. 337 297 1999.
ISSN: ISSN 0264-6021
PubMed: 9882628
DOI: 10.1042/0264-6021:3370297
Page generated: Tue Aug 13 02:15:28 2024

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