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Zinc in PDB 3elf: 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: 3elf 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) 96.67 / 1.31
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 60.638, 119.492, 164.011, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / 16.7

Other elements in 3elf:

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

Zinc binding site 1 out of 2 in 3elf

Go back to Zinc Binding Sites List in 3elf
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:14.4
occ:1.00
 NE2 A:HIS212 2.1 17.9 1.0
ND1 A:HIS252 2.1 13.3 1.0
NE2 A:HIS96 2.1 14.7 1.0
O3 A:2FP350 2.2 14.1 1.0
O4 A:2FP350 2.4 15.2 1.0
O2 A:2FP350 2.6 14.4 1.0
C3 A:2FP350 2.9 14.2 1.0
CE1 A:HIS252 3.0 14.1 1.0
CE1 A:HIS212 3.0 19.9 1.0
CD2 A:HIS212 3.1 17.8 1.0
CE1 A:HIS96 3.1 15.0 1.0
CD2 A:HIS96 3.1 14.6 1.0
C4 A:2FP350 3.1 14.9 1.0
C2 A:2FP350 3.1 14.9 1.0
CG A:HIS252 3.2 13.2 1.0
CB A:HIS252 3.6 13.3 1.0
ND1 A:HIS212 4.1 21.9 1.0
CG A:HIS212 4.1 19.8 1.0
NE2 A:HIS252 4.2 13.8 1.0
ND1 A:HIS96 4.2 15.9 1.0
OD1 A:ASN274 4.2 15.9 1.0
OD1 A:ASP95 4.2 14.9 1.0
CG A:HIS96 4.2 15.5 1.0
OD2 A:ASP95 4.3 16.2 1.0
CD2 A:HIS252 4.3 13.2 1.0
O A:HOH813 4.4 24.4 1.0
C5 A:2FP350 4.5 14.6 1.0
CA A:HIS252 4.5 12.5 1.0
C1 A:2FP350 4.6 16.3 1.0
CG A:ASP95 4.7 14.2 1.0
N A:GLY253 4.8 12.8 1.0

Zinc binding site 2 out of 2 in 3elf

Go back to Zinc Binding Sites List in 3elf
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:17.7
occ:1.00
 ND1 A:HIS344 2.0 17.4 0.5
NE2 A:HIS346 2.1 22.1 1.0
ND1 A:HIS344 2.1 16.8 0.5
O A:HOH455 2.3 19.2 1.0
CE1 A:HIS344 2.9 16.5 0.5
CE1 A:HIS346 3.0 23.5 1.0
CE1 A:HIS344 3.0 16.1 0.5
CD2 A:HIS346 3.1 23.3 1.0
CG A:HIS344 3.1 18.1 0.5
CG A:HIS344 3.2 17.3 0.5
CB A:HIS344 3.5 19.1 0.5
CB A:HIS344 3.5 19.8 0.5
O A:HOH431 3.7 19.5 1.0
CA A:HIS344 4.1 18.8 0.5
CA A:HIS344 4.1 19.4 0.5
NE2 A:HIS344 4.1 17.1 0.5
ND1 A:HIS346 4.1 24.5 1.0
NE2 A:HIS344 4.2 15.4 0.5
CG A:HIS346 4.2 24.8 1.0
CD2 A:HIS344 4.2 17.6 0.5
CD2 A:HIS344 4.2 16.7 0.5
O A:HOH487 4.9 33.6 1.0
C A:HIS344 4.9 20.4 0.5
C A:HIS344 5.0 21.1 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 12:51:37 2024

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