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Zinc in PDB 4a22: Structure of Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase Bound to N-(4-Hydroxybutyl)- Glycolohydroxamic Acid Bis- Phosphate

Enzymatic activity of Structure of Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase Bound to N-(4-Hydroxybutyl)- Glycolohydroxamic Acid Bis- Phosphate

All present enzymatic activity of Structure of Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase Bound to N-(4-Hydroxybutyl)- Glycolohydroxamic Acid Bis- Phosphate:
4.1.2.13;

Protein crystallography data

The structure of Structure of Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase Bound to N-(4-Hydroxybutyl)- Glycolohydroxamic Acid Bis- Phosphate, PDB code: 4a22 was solved by M.Coincon, M.De La Paz Santangelo, P.M.Gest, M.E.Guerin, H.Pham, G.Ryan, S.E.Puckett, J.S.Spencer, M.Gonzalez-Juarrero, R.Daher, A.J.Lenaerts, D.Schnappinger, M.Therisod, S.Ehrt, M.Jackson, J.Sygusch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.42 / 1.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 335.386, 42.977, 102.601, 90.00, 99.39, 90.00
R / Rfree (%) 17.9 / 22.1

Other elements in 4a22:

The structure of Structure of Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase Bound to N-(4-Hydroxybutyl)- Glycolohydroxamic Acid Bis- Phosphate also contains other interesting chemical elements:

Sodium (Na) 6 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase Bound to N-(4-Hydroxybutyl)- Glycolohydroxamic Acid Bis- Phosphate (pdb code 4a22). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase Bound to N-(4-Hydroxybutyl)- Glycolohydroxamic Acid Bis- Phosphate, PDB code: 4a22:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4a22

Go back to Zinc Binding Sites List in 4a22
Zinc binding site 1 out of 2 in the Structure of Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase Bound to N-(4-Hydroxybutyl)- Glycolohydroxamic Acid Bis- Phosphate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase Bound to N-(4-Hydroxybutyl)- Glycolohydroxamic Acid Bis- Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1348

b:36.1
occ:0.30
 NE2 A:HIS212 2.1 41.0 1.0
O01 A:TD41344 2.1 22.4 0.6
ND1 A:HIS252 2.2 35.7 1.0
NE2 A:HIS96 2.2 31.9 1.0
O13 A:TD41344 2.6 23.7 0.6
HO01 A:TD41344 2.8 26.9 0.6
HB3 A:HIS252 2.8 25.6 1.0
CE1 A:HIS212 2.9 49.9 1.0
HE1 A:HIS212 2.9 59.8 1.0
N02 A:TD41344 3.0 27.8 0.6
CE1 A:HIS96 3.0 26.7 1.0
HE1 A:HIS96 3.0 31.9 1.0
CE1 A:HIS252 3.1 39.8 1.0
C12 A:TD41344 3.1 30.7 0.6
CG A:HIS252 3.1 29.1 1.0
HD21 A:ASN274 3.1 29.3 1.0
CD2 A:HIS212 3.2 43.8 1.0
HE1 A:HIS252 3.3 47.6 1.0
CD2 A:HIS96 3.3 36.3 1.0
CB A:HIS252 3.4 21.5 1.0
HD2 A:HIS212 3.5 52.4 1.0
H04A A:TD41344 3.6 38.3 0.6
HD2 A:HIS96 3.6 43.5 1.0
HG22 A:VAL165 3.9 55.7 1.0
H A:GLY253 3.9 27.7 1.0
ND2 A:ASN274 4.0 24.5 1.0
ND1 A:HIS212 4.1 40.2 1.0
HG12 A:VAL165 4.1 50.7 1.0
HA A:HIS252 4.1 21.3 1.0
C03 A:TD41344 4.1 32.5 0.6
HB2 A:HIS252 4.2 25.6 1.0
ND1 A:HIS96 4.2 33.2 1.0
NE2 A:HIS252 4.2 25.1 1.0
CD2 A:HIS252 4.2 25.0 1.0
HD22 A:ASN274 4.2 29.3 1.0
OD1 A:ASP95 4.2 33.7 1.0
CG A:HIS212 4.2 42.5 1.0
C04 A:TD41344 4.3 31.9 0.6
CA A:HIS252 4.4 17.9 1.0
CG A:HIS96 4.4 35.0 1.0
H03A A:TD41344 4.5 38.9 0.6
HB2 A:ASN274 4.5 24.1 1.0
N A:GLY253 4.5 23.2 1.0
OD2 A:ASP95 4.5 35.4 1.0
C14 A:TD41344 4.5 23.9 0.6
HD1 A:HIS212 4.8 48.2 1.0
H03 A:TD41344 4.8 38.9 0.6
HB3 A:ASN274 4.8 24.1 1.0
CG2 A:VAL165 4.8 46.5 1.0
CG A:ASP95 4.8 38.8 1.0
HB A:VAL165 4.9 62.4 1.0
C A:HIS252 4.9 26.7 1.0
H04 A:TD41344 4.9 38.3 0.6
H14A A:TD41344 4.9 28.7 0.6
HD1 A:HIS96 4.9 39.7 1.0
HE2 A:HIS252 4.9 30.0 1.0
CG1 A:VAL165 5.0 42.3 1.0
CG A:ASN274 5.0 28.5 1.0

Zinc binding site 2 out of 2 in 4a22

Go back to Zinc Binding Sites List in 4a22
Zinc binding site 2 out of 2 in the Structure of Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase Bound to N-(4-Hydroxybutyl)- Glycolohydroxamic Acid Bis- Phosphate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase Bound to N-(4-Hydroxybutyl)- Glycolohydroxamic Acid Bis- Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1345

b:45.9
occ:0.30
 NE2 B:HIS212 2.2 51.2 1.0
ND1 B:HIS252 2.2 42.4 1.0
O01 B:TD41344 2.2 23.8 0.3
NE2 B:HIS96 2.3 44.1 1.0
O13 B:TD41344 2.5 23.2 0.3
HO01 B:TD41344 2.8 28.5 0.3
HB3 B:HIS252 2.9 31.3 1.0
HD21 B:ASN274 2.9 41.1 1.0
CE1 B:HIS212 2.9 51.7 1.0
HE1 B:HIS212 3.0 62.0 1.0
N02 B:TD41344 3.0 32.0 0.3
HD2 B:HIS96 3.0 52.0 1.0
CD2 B:HIS96 3.0 43.5 1.0
C12 B:TD41344 3.1 31.4 0.3
CE1 B:HIS252 3.1 42.0 1.0
CG B:HIS252 3.2 35.0 1.0
CD2 B:HIS212 3.3 49.7 1.0
HE1 B:HIS252 3.3 50.3 1.0
CE1 B:HIS96 3.4 43.0 1.0
CB B:HIS252 3.5 26.1 1.0
HD2 B:HIS212 3.6 59.5 1.0
ND2 B:ASN274 3.6 34.4 1.0
HE1 B:HIS96 3.7 51.4 1.0
H B:GLY253 3.9 61.9 1.0
HA B:HIS252 3.9 26.9 1.0
HD22 B:ASN274 4.0 41.1 1.0
HG22 B:VAL165 4.0 53.2 1.0
HG12 B:VAL165 4.0 51.2 1.0
ND1 B:HIS212 4.1 52.9 1.0
HB2 B:ASN274 4.2 25.6 1.0
H04 B:TD41344 4.2 39.3 0.3
HB2 B:HIS252 4.2 31.3 1.0
C03 B:TD41344 4.3 30.6 0.3
NE2 B:HIS252 4.3 32.4 1.0
CG B:HIS96 4.3 40.4 1.0
CA B:HIS252 4.3 22.5 1.0
CG B:HIS212 4.3 51.1 1.0
CD2 B:HIS252 4.3 34.4 1.0
OD1 B:ASP95 4.3 47.2 1.0
HB3 B:ASN274 4.4 25.6 1.0
ND1 B:HIS96 4.4 43.9 1.0
OD2 B:ASP95 4.5 41.3 1.0
C14 B:TD41344 4.5 27.7 0.3
CG B:ASN274 4.6 28.7 1.0
N B:GLY253 4.6 51.7 1.0
CB B:ASN274 4.6 21.4 1.0
H03A B:TD41344 4.6 36.6 0.3
C04 B:TD41344 4.7 32.7 0.3
H05A B:TD41344 4.7 39.7 0.3
HD1 B:HIS212 4.8 63.3 1.0
CG B:ASP95 4.8 46.6 1.0
H14A B:TD41344 4.9 33.3 0.3
O15 B:TD41344 4.9 28.5 0.3
H03 B:TD41344 4.9 36.6 0.3
CG2 B:VAL165 4.9 44.5 1.0
CG1 B:VAL165 4.9 42.8 1.0
C B:HIS252 4.9 28.1 1.0

Reference:

M.De La Paz Santangelo, P.M.Gest, M.E.Guerin, M.Coincon, H.Pham, G.Ryan, S.E.Puckett, J.S.Spencer, M.Gonzalez-Juarrero, R.Daher, A.J.Lenaerts, D.Schnappinger, M.Therisod, S.Ehrt, J.Sygusch, M.Jackson. Glycolytic and Non-Glycolytic Functions of Mycobacterium Tuberculosis Fructose-1,6-Bisphosphate Aldolase, An Essential Enzyme Produced By Replicating and Non-Replicating Bacilli. J. Biol. Chem. V. 286 40219 2011.
ISSN: ESSN 1083-351X
PubMed: 21949126
DOI: 10.1074/JBC.M111.259440
Page generated: Sat Oct 26 18:48:29 2024

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