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Zinc in PDB 3ekl: 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: 3ekl 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) 97.10 / 1.51
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 61.285, 120.227, 164.823, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 17.6

Other elements in 3ekl:

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 3ekl). 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: 3ekl:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3ekl

Go back to Zinc Binding Sites List in 3ekl
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:Zn352

b:15.8
occ:1.00
 NE2 A:HIS212 2.0 18.2 1.0
NE2 A:HIS96 2.1 19.9 1.0
ND1 A:HIS252 2.1 16.4 1.0
O3 A:13P351 2.1 16.4 0.7
O2 A:13P351 2.2 21.3 0.7
O2 A:13P350 2.5 14.3 0.3
C3 A:13P351 2.9 20.7 0.7
CE1 A:HIS212 2.9 20.4 1.0
C2 A:13P351 2.9 24.0 0.7
CE1 A:HIS252 3.0 18.7 1.0
CE1 A:HIS96 3.0 18.0 1.0
CD2 A:HIS96 3.1 20.4 1.0
CD2 A:HIS212 3.2 19.3 1.0
CG A:HIS252 3.2 18.0 1.0
C2 A:13P350 3.5 12.7 0.3
CB A:HIS252 3.6 18.9 1.0
C3 A:13P350 3.7 13.0 0.3
O3 A:13P350 3.8 11.8 0.3
O A:HOH706 3.9 11.5 1.0
OD1 A:ASN274 4.0 21.9 1.0
ND1 A:HIS212 4.0 20.0 1.0
NE2 A:HIS252 4.1 17.8 1.0
OD1 A:ASP95 4.1 20.6 1.0
ND1 A:HIS96 4.2 19.1 1.0
CG A:HIS96 4.2 18.7 1.0
CG A:HIS212 4.2 19.5 1.0
CD2 A:HIS252 4.3 18.0 1.0
C1 A:13P351 4.3 26.4 0.7
OD2 A:ASP95 4.4 20.1 1.0
CA A:HIS252 4.5 18.8 1.0
N A:GLY253 4.7 18.8 1.0
CG A:ASP95 4.7 19.3 1.0
O1 A:13P351 4.8 32.9 0.7
C1 A:13P350 4.8 13.3 0.3
CG A:ASN274 4.9 18.3 1.0
CG1 A:VAL165 5.0 24.0 1.0

Zinc binding site 2 out of 2 in 3ekl

Go back to Zinc Binding Sites List in 3ekl
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:Zn353

b:14.7
occ:1.00
 ND1 A:HIS344 2.0 17.4 0.5
NE2 A:HIS346 2.1 20.0 1.0
ND1 A:HIS344 2.1 18.4 0.5
O A:HOH459 2.4 16.4 1.0
CE1 A:HIS346 3.0 23.6 1.0
CE1 A:HIS344 3.0 17.1 0.5
CE1 A:HIS344 3.0 19.1 0.5
CG A:HIS344 3.1 18.5 0.5
CD2 A:HIS346 3.1 23.7 1.0
CG A:HIS344 3.1 19.2 0.5
CB A:HIS344 3.5 19.8 0.5
CB A:HIS344 3.5 20.4 0.5
O A:HOH433 3.8 14.6 1.0
CA A:HIS344 4.0 20.4 0.5
CA A:HIS344 4.1 20.9 0.5
ND1 A:HIS346 4.1 24.6 1.0
NE2 A:HIS344 4.1 17.7 0.5
NE2 A:HIS344 4.2 19.2 0.5
CD2 A:HIS344 4.2 17.8 0.5
CG A:HIS346 4.2 25.8 1.0
CD2 A:HIS344 4.2 18.4 0.5
C A:HIS344 4.8 21.4 0.5
O A:HOH493 4.9 25.8 1.0
C A:HIS344 4.9 22.0 0.5
O A:HIS344 4.9 21.4 0.5

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

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