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Zinc in PDB 2isw: Structure of Giardia Fructose-1,6-Biphosphate Aldolase in Complex with Phosphoglycolohydroxamate

Enzymatic activity of Structure of Giardia Fructose-1,6-Biphosphate Aldolase in Complex with Phosphoglycolohydroxamate

All present enzymatic activity of Structure of Giardia Fructose-1,6-Biphosphate Aldolase in Complex with Phosphoglycolohydroxamate:
4.1.2.13;

Protein crystallography data

The structure of Structure of Giardia Fructose-1,6-Biphosphate Aldolase in Complex with Phosphoglycolohydroxamate, PDB code: 2isw was solved by A.Galkin, O.Herzberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.75
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 90.020, 90.050, 166.090, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 22.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Giardia Fructose-1,6-Biphosphate Aldolase in Complex with Phosphoglycolohydroxamate (pdb code 2isw). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of Giardia Fructose-1,6-Biphosphate Aldolase in Complex with Phosphoglycolohydroxamate, PDB code: 2isw:

Zinc binding site 1 out of 1 in 2isw

Go back to Zinc Binding Sites List in 2isw
Zinc binding site 1 out of 1 in the Structure of Giardia Fructose-1,6-Biphosphate Aldolase in Complex with Phosphoglycolohydroxamate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Giardia Fructose-1,6-Biphosphate Aldolase in Complex with Phosphoglycolohydroxamate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn326

b:56.2
occ:1.00
 NE2 A:HIS84 2.1 40.7 1.0
ND1 A:HIS210 2.2 48.1 1.0
NE2 A:HIS178 2.3 58.7 1.0
O1 A:PGH325 2.5 50.0 1.0
O2 A:PGH325 2.6 52.4 1.0
CE1 A:HIS178 3.0 69.1 1.0
CD2 A:HIS84 3.1 45.4 1.0
CE1 A:HIS210 3.1 48.7 1.0
CE1 A:HIS84 3.1 38.1 1.0
CG A:HIS210 3.2 43.5 1.0
C1 A:PGH325 3.2 59.8 1.0
CD2 A:HIS178 3.4 51.9 1.0
N2 A:PGH325 3.5 56.2 1.0
CB A:HIS210 3.5 34.2 1.0
ND2 A:ASN253 4.0 38.9 1.0
ND1 A:HIS178 4.2 64.3 1.0
OD2 A:ASP83 4.2 29.6 1.0
NE2 A:HIS210 4.2 32.5 1.0
ND1 A:HIS84 4.2 44.2 1.0
CG A:HIS84 4.2 45.0 1.0
CD2 A:HIS210 4.3 40.5 1.0
OD1 A:ASP83 4.3 28.9 1.0
CG A:HIS178 4.4 65.3 1.0
CA A:HIS210 4.4 31.0 1.0
N A:GLY211 4.6 33.9 1.0
CG A:ASP83 4.7 27.1 1.0
C2 A:PGH325 4.9 58.9 1.0
O A:HOH487 4.9 59.8 1.0

Reference:

A.Galkin, L.Kulakova, E.Melamud, L.Li, C.Wu, P.Mariano, D.Dunaway-Mariano, T.E.Nash, O.Herzberg. Characterization, Kinetics, and Crystal Structures of Fructose-1,6-Bisphosphate Aldolase From the Human Parasite, Giardia Lamblia. J.Biol.Chem. V. 282 4859 2007.
ISSN: ISSN 0021-9258
PubMed: 17166851
DOI: 10.1074/JBC.M609534200
Page generated: Thu Oct 17 00:59:00 2024

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