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Calcium in PDB 1g9g: Xtal-Structure of the Free Native Cellulase CEL48F

Enzymatic activity of Xtal-Structure of the Free Native Cellulase CEL48F

All present enzymatic activity of Xtal-Structure of the Free Native Cellulase CEL48F:
3.2.1.4;

Protein crystallography data

The structure of Xtal-Structure of the Free Native Cellulase CEL48F, PDB code: 1g9g was solved by G.Parsiegla, C.Tardif, J.P.Belaich, H.Driguez, R.Haser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.59 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 61.530, 84.770, 122.120, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 19.5

Other elements in 1g9g:

The structure of Xtal-Structure of the Free Native Cellulase CEL48F also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Xtal-Structure of the Free Native Cellulase CEL48F (pdb code 1g9g). 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 Xtal-Structure of the Free Native Cellulase CEL48F, PDB code: 1g9g:

Calcium binding site 1 out of 1 in 1g9g

Go back to Calcium Binding Sites List in 1g9g
Calcium binding site 1 out of 1 in the Xtal-Structure of the Free Native Cellulase CEL48F


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Xtal-Structure of the Free Native Cellulase CEL48F within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca630

b:17.0
occ:1.00
OE2 A:GLU190 2.3 14.7 1.0
O A:GLN185 2.3 13.3 1.0
O A:HOH971 2.4 21.2 1.0
O A:HOH1026 2.4 18.1 1.0
OD2 A:ASP405 2.4 17.4 1.0
OE1 A:GLN185 2.6 22.3 1.0
OE1 A:GLU190 2.7 17.4 1.0
CD A:GLU190 2.9 16.2 1.0
C A:GLN185 3.5 14.6 1.0
CG A:ASP405 3.5 18.2 1.0
CD A:GLN185 3.7 21.6 1.0
CB A:ASP405 4.0 17.6 1.0
CB A:GLN185 4.1 16.9 1.0
CA A:GLN185 4.1 16.1 1.0
NH2 A:ARG549 4.2 17.8 1.0
CG A:GLU190 4.4 13.9 1.0
N A:SER187 4.4 13.2 1.0
CG A:GLN185 4.4 20.1 1.0
O A:HOH889 4.5 37.2 1.0
OD1 A:ASP405 4.6 17.8 1.0
N A:GLU186 4.6 13.2 1.0
O A:HOH936 4.7 43.6 1.0
OG A:SER187 4.7 12.8 1.0
NE2 A:GLN185 4.7 21.7 1.0
CA A:GLU186 4.8 13.1 1.0
O A:HOH895 4.8 41.1 1.0
CB A:SER187 4.8 12.9 1.0
O A:HOH729 4.9 24.9 1.0

Reference:

G.Parsiegla, C.Reverbel, C.Tardif, H.Driguez, R.Haser. Structures of Mutants of Cellulase CEL48F of Clostridium Cellulolyticum in Complex with Long Hemithiocellooligosaccharides Give Rise to A New View of the Substrate Pathway During Processive Action J.Mol.Biol. V. 375 499 2008.
ISSN: ISSN 0022-2836
PubMed: 18035374
DOI: 10.1016/J.JMB.2007.10.039
Page generated: Sat Dec 12 02:57:30 2020

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