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Zinc in PDB 1a72: An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad

Enzymatic activity of An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad

All present enzymatic activity of An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad:
1.1.1.1;

Protein crystallography data

The structure of An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad, PDB code: 1a72 was solved by T.D.Colby, B.J.Bahnson, J.K.Chin, J.P.Klinman, B.M.Goldstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.60
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 55.500, 74.200, 179.200, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 30

Zinc Binding Sites:

The binding sites of Zinc atom in the An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad (pdb code 1a72). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad, PDB code: 1a72:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1a72

Go back to Zinc Binding Sites List in 1a72
Zinc binding site 1 out of 2 in the An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn376

b:25.8
occ:1.00
O A:HOH401 1.7 31.0 1.0
NE2 A:HIS67 2.0 13.5 1.0
SG A:CYS174 2.3 7.2 1.0
SG A:CYS46 2.4 10.5 1.0
CE1 A:HIS67 2.9 12.5 1.0
OG A:SER48 3.0 20.7 1.0
CD2 A:HIS67 3.2 12.4 1.0
CB A:CYS46 3.5 9.0 1.0
CB A:CYS174 3.6 9.3 1.0
CB A:SER48 3.7 20.3 1.0
ND1 A:HIS67 4.1 12.7 1.0
CG A:HIS67 4.2 12.7 1.0
N A:SER48 4.6 17.8 1.0
C4N A:PAD378 4.6 35.2 1.0
CA A:SER48 4.8 18.5 1.0
CA A:CYS46 4.9 11.1 1.0
CA A:CYS174 4.9 12.6 1.0
CZ2 A:TRP93 5.0 8.4 1.0

Zinc binding site 2 out of 2 in 1a72

Go back to Zinc Binding Sites List in 1a72
Zinc binding site 2 out of 2 in the An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn377

b:20.6
occ:1.00
SG A:CYS100 2.1 17.8 1.0
SG A:CYS111 2.3 17.4 1.0
SG A:CYS97 2.4 13.1 1.0
SG A:CYS103 2.4 14.2 1.0
CB A:CYS100 3.5 16.4 1.0
CB A:CYS103 3.5 15.1 1.0
CB A:CYS111 3.5 15.8 1.0
N A:CYS97 3.6 11.8 1.0
CB A:CYS97 3.6 12.3 1.0
N A:CYS100 3.8 18.0 1.0
CA A:CYS111 3.9 17.6 1.0
N A:LEU112 3.9 20.0 1.0
N A:GLY98 4.0 17.4 1.0
CA A:CYS97 4.0 12.5 1.0
N A:CYS103 4.2 13.7 1.0
CA A:CYS100 4.2 16.2 1.0
N A:LYS99 4.3 20.3 1.0
C A:CYS97 4.3 13.9 1.0
C A:CYS111 4.4 19.5 1.0
CA A:CYS103 4.4 14.6 1.0
C A:GLN96 4.6 12.2 1.0
N A:LYS113 4.7 16.7 1.0
CA A:GLN96 4.8 12.7 1.0
CA A:GLY98 4.9 18.1 1.0
C A:CYS100 4.9 16.9 1.0
C A:LYS99 4.9 19.8 1.0
CB A:LEU112 4.9 16.9 1.0
CA A:LEU112 4.9 19.7 1.0

Reference:

T.D.Colby, B.J.Bahnson, J.K.Chin, J.P.Klinman, B.M.Goldstein. Active Site Modifications in A Double Mutant of Liver Alcohol Dehydrogenase: Structural Studies of Two Enzyme-Ligand Complexes. Biochemistry V. 37 9295 1998.
ISSN: ISSN 0006-2960
PubMed: 9649310
DOI: 10.1021/BI973184B
Page generated: Wed Dec 16 02:44:28 2020

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