Atomistry » Magnesium » PDB 1g7t-1gol » 1g9g
Atomistry »
  Magnesium »
    PDB 1g7t-1gol »
      1g9g »

Magnesium 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:

Calcium (Ca) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium 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 Magnesium atom.
In total only one binding site of Magnesium was determined in the Xtal-Structure of the Free Native Cellulase CEL48F, PDB code: 1g9g:

Magnesium binding site 1 out of 1 in 1g9g

Go back to Magnesium Binding Sites List in 1g9g
Magnesium 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 Magnesium with other atoms in the Mg 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:Mg631

b:47.1
occ:1.00
O A:HOH869 2.2 41.5 1.0
O A:HOH772 2.2 30.4 1.0
OH A:TYR323 2.8 18.4 1.0
O A:TRP298 2.8 12.2 1.0
NE1 A:TRP298 3.3 16.0 1.0
CE2 A:TYR323 3.4 15.3 1.0
CD1 A:TRP298 3.4 14.9 1.0
CZ A:TYR323 3.5 15.8 1.0
CE2 A:TRP298 3.8 15.4 1.0
O A:HOH828 3.8 41.6 1.0
CA A:ALA228 3.9 9.0 1.0
C A:TRP298 4.0 12.6 1.0
CG A:TRP298 4.0 13.9 1.0
O A:HOH860 4.0 38.6 1.0
CB A:ALA228 4.0 9.4 1.0
CD2 A:TRP298 4.2 15.0 1.0
O A:ASN227 4.3 10.4 1.0
O A:HOH917 4.5 22.3 0.5
CZ2 A:TRP298 4.5 16.6 1.0
CA A:TRP298 4.6 11.8 1.0
CD A:PRO229 4.6 7.2 1.0
CD2 A:TYR323 4.7 13.7 1.0
CB A:TYR299 4.7 14.5 1.0
CE1 A:TYR323 4.8 15.8 1.0
CB A:TRP298 4.9 12.7 1.0
N A:ALA228 4.9 8.5 1.0
C A:ALA228 5.0 8.6 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: Mon Dec 14 05:57:38 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy