Atomistry » Zinc » PDB 3eju-3eyd » 3ekz
Atomistry »
  Zinc »
    PDB 3eju-3eyd »
      3ekz »

Zinc in PDB 3ekz: Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase

Enzymatic activity of Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase

All present enzymatic activity of Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase:
4.1.2.13;

Protein crystallography data

The structure of Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase, PDB code: 3ekz was solved by S.Pegan, K.Rukseree, S.G.Franzblau, A.D.Mesecar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.90 / 2.07
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 61.220, 120.486, 164.327, 90.00, 90.00, 90.00
R / Rfree (%) 15.8 / 18

Other elements in 3ekz:

The structure of Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase also contains other interesting chemical elements:

Sodium (Na) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase (pdb code 3ekz). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase, PDB code: 3ekz:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3ekz

Go back to Zinc Binding Sites List in 3ekz
Zinc binding site 1 out of 2 in the Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn354

b:35.6
occ:1.00
 NE2 A:HIS96 2.1 26.6 1.0
NE2 A:HIS212 2.1 22.9 1.0
O3 A:13P351 2.3 17.6 0.7
ND1 A:HIS252 2.3 17.0 1.0
O2 A:13P351 2.6 20.4 0.7
O2 A:13P350 2.8 17.6 0.3
CE1 A:HIS212 3.0 24.0 1.0
C3 A:13P351 3.0 20.6 0.7
CD2 A:HIS96 3.0 21.7 1.0
CE1 A:HIS96 3.1 25.1 1.0
CD2 A:HIS212 3.1 21.7 1.0
C2 A:13P351 3.1 21.4 0.7
CE1 A:HIS252 3.2 17.5 1.0
CG A:HIS252 3.4 17.9 1.0
O3 A:13P350 3.5 19.2 0.3
C1 A:G3P352 3.5 47.2 1.0
CB A:HIS252 3.7 17.5 1.0
C2 A:13P350 3.8 17.5 0.3
O1 A:G3P352 3.9 48.9 1.0
ND1 A:HIS212 4.1 22.2 1.0
CG A:HIS212 4.2 20.8 1.0
ND1 A:HIS96 4.2 25.9 1.0
CG A:HIS96 4.2 23.4 1.0
OD1 A:ASP95 4.2 18.9 1.0
OD1 A:ASN274 4.2 21.9 1.0
C3 A:13P350 4.2 17.2 0.3
OD2 A:ASP95 4.3 21.0 1.0
C2 A:G3P352 4.3 46.1 1.0
NE2 A:HIS252 4.3 17.7 1.0
CD2 A:HIS252 4.5 16.0 1.0
C1 A:13P351 4.6 20.4 0.7
CA A:HIS252 4.7 17.5 1.0
CG A:ASP95 4.7 20.2 1.0
N A:GLY253 4.8 17.5 1.0
CG2 A:VAL165 4.9 19.2 1.0
CG1 A:VAL165 5.0 20.6 1.0
O2 A:G3P352 5.0 45.4 1.0

Zinc binding site 2 out of 2 in 3ekz

Go back to Zinc Binding Sites List in 3ekz
Zinc binding site 2 out of 2 in the Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn355

b:24.8
occ:1.00
 ND1 A:HIS344 2.0 15.2 1.0
NE2 A:HIS346 2.0 24.0 1.0
O A:HOH459 2.4 26.2 1.0
CE1 A:HIS346 2.9 24.9 1.0
CE1 A:HIS344 2.9 17.3 1.0
CD2 A:HIS346 3.1 25.6 1.0
CG A:HIS344 3.1 18.1 1.0
CB A:HIS344 3.5 18.9 1.0
O A:HOH433 3.7 20.6 1.0
CA A:HIS344 4.0 19.8 1.0
ND1 A:HIS346 4.1 25.4 1.0
NE2 A:HIS344 4.1 16.5 1.0
CG A:HIS346 4.2 27.4 1.0
CD2 A:HIS344 4.2 15.2 1.0
C A:HIS344 4.8 21.5 1.0
O A:HOH493 4.9 33.6 1.0
O A:HIS344 4.9 20.1 1.0

Reference:

S.D.Pegan, K.Rukseree, S.G.Franzblau, A.D.Mesecar. Structural Basis For Catalysis of A Tetrameric Class Iia Fructose 1,6-Bisphosphate Aldolase From Mycobacterium Tuberculosis J.Mol.Biol. V. 386 1038 2009.
ISSN: ISSN 0022-2836
PubMed: 19167403
DOI: 10.1016/J.JMB.2009.01.003
Page generated: Thu Oct 24 12:51:14 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy