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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: Wed Dec 16 04:16:29 2020

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