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Zinc in PDB 1f8f: Crystal Structure of Benzyl Alcohol Dehydrogenase From Acinetobacter Calcoaceticus

Enzymatic activity of Crystal Structure of Benzyl Alcohol Dehydrogenase From Acinetobacter Calcoaceticus

All present enzymatic activity of Crystal Structure of Benzyl Alcohol Dehydrogenase From Acinetobacter Calcoaceticus:
1.1.1.90;

Protein crystallography data

The structure of Crystal Structure of Benzyl Alcohol Dehydrogenase From Acinetobacter Calcoaceticus, PDB code: 1f8f was solved by J.C.Beauchamp, D.Gillooly, J.Warwicker, C.A.Fewson, A.J.Lapthorn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.20
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 82.294, 96.985, 103.909, 90.00, 90.00, 90.00
R / Rfree (%) 19.7 / 26.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Benzyl Alcohol Dehydrogenase From Acinetobacter Calcoaceticus (pdb code 1f8f). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Benzyl Alcohol Dehydrogenase From Acinetobacter Calcoaceticus, PDB code: 1f8f:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1f8f

Go back to Zinc Binding Sites List in 1f8f
Zinc binding site 1 out of 2 in the Crystal Structure of Benzyl Alcohol Dehydrogenase From Acinetobacter Calcoaceticus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Benzyl Alcohol Dehydrogenase From Acinetobacter Calcoaceticus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn372

b:42.4
occ:1.00
SG A:CYS173 2.2 26.9 1.0
NE2 A:HIS65 2.2 35.4 1.0
O A:EOH374 2.4 46.0 1.0
SG A:CYS44 2.4 32.4 1.0
CD2 A:HIS65 3.2 29.9 1.0
CE1 A:HIS65 3.2 31.1 1.0
C1 A:EOH374 3.4 50.9 1.0
CB A:CYS173 3.4 27.7 1.0
CB A:CYS44 3.5 35.7 1.0
C5N A:NAD375 3.8 51.5 1.0
OG1 A:THR46 3.9 41.3 1.0
CB A:THR46 4.1 40.4 1.0
C4N A:NAD375 4.2 50.3 1.0
OE2 A:GLU66 4.3 33.6 1.0
CG A:HIS65 4.4 29.9 1.0
ND1 A:HIS65 4.4 31.1 1.0
C6N A:NAD375 4.5 52.0 1.0
N A:GLY174 4.6 27.5 1.0
CA A:CYS173 4.7 27.6 1.0
C2 A:EOH374 4.8 50.0 1.0
C A:CYS173 4.9 27.4 1.0
CG2 A:THR46 5.0 37.6 1.0
CA A:CYS44 5.0 35.3 1.0

Zinc binding site 2 out of 2 in 1f8f

Go back to Zinc Binding Sites List in 1f8f
Zinc binding site 2 out of 2 in the Crystal Structure of Benzyl Alcohol Dehydrogenase From Acinetobacter Calcoaceticus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Benzyl Alcohol Dehydrogenase From Acinetobacter Calcoaceticus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn373

b:26.0
occ:1.00
SG A:CYS100 2.3 24.1 1.0
SG A:CYS94 2.3 25.1 1.0
SG A:CYS108 2.3 21.1 1.0
SG A:CYS97 2.4 18.6 1.0
CB A:CYS108 3.1 22.6 1.0
CB A:CYS94 3.4 28.4 1.0
CB A:CYS97 3.4 21.8 1.0
CB A:CYS100 3.5 24.0 1.0
N A:GLY95 3.5 30.7 1.0
CA A:CYS108 3.6 22.7 1.0
N A:CYS94 3.8 28.0 1.0
N A:CYS97 3.8 25.6 1.0
CA A:CYS94 3.9 29.1 1.0
N A:SER109 4.1 29.9 1.0
C A:CYS94 4.1 29.9 1.0
CA A:CYS97 4.1 25.4 1.0
N A:CYS100 4.3 21.4 1.0
C A:CYS108 4.3 25.3 1.0
N A:LYS96 4.3 30.6 1.0
CA A:CYS100 4.5 21.9 1.0
CA A:GLY95 4.5 31.6 1.0
N A:GLU110 4.7 34.8 1.0
O A:HOH553 4.8 36.2 1.0
C A:CYS97 4.8 24.8 1.0
C A:LYS96 4.9 31.9 1.0
N A:CYS108 4.9 23.3 1.0
C A:TYR93 4.9 29.7 1.0
C A:GLY95 5.0 30.8 1.0
OG A:SER109 5.0 33.1 1.0

Reference:

J.C.Beauchamp, D.Gillooly, J.Warwicker, C.A.Fewson, A.J.Lapthorn. Crystal Structure of Benzyl Alcohol Dehydrogenase From Acinetobacter Calcoaceticus To Be Published.
Page generated: Wed Dec 16 02:49:07 2020

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