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Zinc in PDB 3zdr: Structure of the Alcohol Dehydrogenase (Adh) Domain of A Bifunctional Adhe Dehydrogenase From Geobacillus Thermoglucosidasius Ncimb 11955

Enzymatic activity of Structure of the Alcohol Dehydrogenase (Adh) Domain of A Bifunctional Adhe Dehydrogenase From Geobacillus Thermoglucosidasius Ncimb 11955

All present enzymatic activity of Structure of the Alcohol Dehydrogenase (Adh) Domain of A Bifunctional Adhe Dehydrogenase From Geobacillus Thermoglucosidasius Ncimb 11955:
1.1.1.1; 1.2.1.10;

Protein crystallography data

The structure of Structure of the Alcohol Dehydrogenase (Adh) Domain of A Bifunctional Adhe Dehydrogenase From Geobacillus Thermoglucosidasius Ncimb 11955, PDB code: 3zdr was solved by J.Extance, S.J.Crennell, K.Eley, R.Cripps, D.W.Hough, M.J.Danson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.294 / 2.504
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 73.721, 96.588, 58.200, 90.00, 90.00, 90.00
R / Rfree (%) 17.44 / 23.96

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of the Alcohol Dehydrogenase (Adh) Domain of A Bifunctional Adhe Dehydrogenase From Geobacillus Thermoglucosidasius Ncimb 11955 (pdb code 3zdr). 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 the Alcohol Dehydrogenase (Adh) Domain of A Bifunctional Adhe Dehydrogenase From Geobacillus Thermoglucosidasius Ncimb 11955, PDB code: 3zdr:

Zinc binding site 1 out of 1 in 3zdr

Go back to Zinc Binding Sites List in 3zdr
Zinc binding site 1 out of 1 in the Structure of the Alcohol Dehydrogenase (Adh) Domain of A Bifunctional Adhe Dehydrogenase From Geobacillus Thermoglucosidasius Ncimb 11955


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Alcohol Dehydrogenase (Adh) Domain of A Bifunctional Adhe Dehydrogenase From Geobacillus Thermoglucosidasius Ncimb 11955 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1870

b:55.4
occ:0.69
 OD1 A:ASP661 2.0 63.4 1.0
O1 A:GOL1872 2.0 63.8 1.0
OD2 A:ASP661 2.1 61.8 1.0
NE2 A:HIS730 2.1 57.9 1.0
NE2 A:HIS665 2.1 49.6 1.0
NE2 A:HIS744 2.1 61.4 1.0
CG A:ASP661 2.3 55.4 1.0
CE1 A:HIS730 2.8 56.7 1.0
HE1 A:HIS730 2.8 68.0 1.0
CD2 A:HIS744 2.9 51.1 1.0
HD2 A:HIS744 2.9 61.3 1.0
CE1 A:HIS665 3.0 53.3 1.0
CD2 A:HIS665 3.1 41.4 1.0
HE1 A:HIS665 3.1 64.0 1.0
CD2 A:HIS730 3.2 60.7 1.0
C1 A:GOL1872 3.3 65.7 1.0
HD2 A:HIS665 3.3 49.6 1.0
CE1 A:HIS744 3.3 60.6 1.0
H11 A:GOL1872 3.5 78.8 1.0
H2 A:GOL1872 3.5 85.6 1.0
HD2 A:HIS730 3.6 72.8 1.0
HE1 A:HIS744 3.6 72.7 1.0
CB A:ASP661 3.9 31.3 1.0
H32 A:GOL1872 3.9 87.5 1.0
C2 A:GOL1872 3.9 71.3 1.0
ND1 A:HIS730 4.0 44.5 1.0
ND1 A:HIS665 4.1 45.3 1.0
H12 A:GOL1872 4.1 78.8 1.0
CG A:HIS665 4.1 45.1 1.0
CG A:HIS744 4.2 53.6 1.0
HB2 A:ASP661 4.3 37.5 1.0
CG A:HIS730 4.3 63.0 1.0
HB3 A:ASP661 4.3 37.5 1.0
ND1 A:HIS744 4.3 59.3 1.0
OD1 A:ASN748 4.3 50.0 1.0
C3 A:GOL1872 4.4 72.9 1.0
HA A:ASP661 4.5 42.5 1.0
O A:ASP661 4.5 34.0 1.0
CA A:ASP661 4.7 35.4 1.0
HD1 A:HIS730 4.7 53.4 1.0
HD1 A:HIS665 4.8 54.3 1.0
H31 A:GOL1872 4.8 87.5 1.0
C A:ASP661 4.9 37.1 1.0
HD11 A:LEU726 4.9 51.5 1.0
HA A:THR609 4.9 53.2 1.0
HB A:THR664 5.0 55.7 1.0

Reference:

J.Extance, S.J.Crennell, K.Eley, R.Cripps, D.W.Hough, M.J.Danson. Structure of A Bifunctional Alcohol Dehydrogenase Involved in Bioethanol Generation in Geobacillus Thermoglucosidasius Acta Crystallogr.,Sect.D V. 69 2104 2013.
ISSN: ISSN 0907-4449
PubMed: 24100328
DOI: 10.1107/S0907444913020349
Page generated: Sat Oct 26 18:26:57 2024

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