Zinc in PDB 6nbb: Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev

Enzymatic activity of Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev

All present enzymatic activity of Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev:
1.1.1.1;

Zinc Binding Sites:

The binding sites of Zinc atom in the Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev (pdb code 6nbb). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev, PDB code: 6nbb:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 6nbb

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Zinc binding site 1 out of 4 in the Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn402

b:74.6
occ:1.00
NE2 A:HIS67 2.0 75.9 1.0
SG A:CYS46 2.2 80.1 1.0
SG A:CYS174 2.3 71.3 1.0
CB A:CYS46 2.5 80.1 1.0
CD2 A:HIS67 2.9 75.9 1.0
CE1 A:HIS67 3.0 75.9 1.0
CB A:CYS174 3.2 71.3 1.0
OE1 A:GLU68 3.3 75.8 1.0
CA A:CYS46 3.9 80.1 1.0
CG A:HIS67 4.0 75.9 1.0
ND1 A:HIS67 4.0 75.9 1.0
C5N A:NAD401 4.1 62.3 1.0
CD A:GLU68 4.2 75.8 1.0
CB A:GLU68 4.2 75.8 1.0
CA A:CYS174 4.5 71.3 1.0
OG A:SER48 4.5 81.0 1.0
C6N A:NAD401 4.6 62.3 1.0
CB A:SER48 4.6 81.0 1.0
CG A:GLU68 4.7 75.8 1.0
N A:CYS46 4.7 80.1 1.0
C A:CYS174 4.7 71.3 1.0
C A:CYS46 4.8 80.1 1.0
N A:GLY175 4.9 65.3 1.0
NH2 A:ARG369 4.9 74.0 1.0
C4N A:NAD401 5.0 62.3 1.0

Zinc binding site 2 out of 4 in 6nbb

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Zinc binding site 2 out of 4 in the Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn403

b:74.6
occ:1.00
SG A:CYS103 2.1 70.0 1.0
SG A:CYS111 2.2 70.3 1.0
SG A:CYS100 2.3 69.7 1.0
SG A:CYS97 2.3 70.1 1.0
CB A:CYS111 2.7 70.3 1.0
CA A:CYS111 3.4 70.3 1.0
N A:CYS97 3.4 70.1 1.0
CB A:CYS97 3.4 70.1 1.0
CB A:CYS100 3.6 69.7 1.0
CB A:CYS103 3.6 70.0 1.0
CA A:CYS97 4.0 70.1 1.0
N A:LEU112 4.1 71.7 1.0
C A:CYS111 4.3 70.3 1.0
N A:CYS103 4.3 70.0 1.0
N A:GLY98 4.3 70.9 1.0
C A:GLN96 4.4 67.4 1.0
N A:CYS111 4.5 70.3 1.0
CA A:CYS103 4.5 70.0 1.0
CA A:GLN96 4.5 67.4 1.0
O A:PRO95 4.6 68.3 1.0
N A:CYS100 4.6 69.7 1.0
CA A:CYS100 4.7 69.7 1.0
C A:CYS97 4.7 70.1 1.0

Zinc binding site 3 out of 4 in 6nbb

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Zinc binding site 3 out of 4 in the Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn402

b:96.3
occ:1.00
NE2 B:HIS67 2.0 76.7 1.0
SG B:CYS46 2.3 79.8 1.0
SG B:CYS174 2.3 70.7 1.0
CD2 B:HIS67 2.7 76.7 1.0
CB B:CYS46 3.0 79.8 1.0
OE2 B:GLU68 3.1 76.5 1.0
CE1 B:HIS67 3.2 76.7 1.0
CB B:CYS174 3.2 70.7 1.0
CG B:GLU68 3.5 76.5 1.0
C5N B:NAD401 3.7 42.0 1.0
CD B:GLU68 3.7 76.5 1.0
CG B:HIS67 4.0 76.7 1.0
ND1 B:HIS67 4.1 76.7 1.0
C6N B:NAD401 4.3 42.0 1.0
CA B:CYS46 4.4 79.8 1.0
OG B:SER48 4.4 81.4 1.0
C4N B:NAD401 4.5 42.0 1.0
CA B:CYS174 4.5 70.7 1.0
CB B:SER48 4.7 81.4 1.0
C B:CYS174 4.7 70.7 1.0
N B:GLY175 4.7 64.9 1.0
CB B:GLU68 5.0 76.5 1.0
OE1 B:GLU68 5.0 76.5 1.0

Zinc binding site 4 out of 4 in 6nbb

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Zinc binding site 4 out of 4 in the Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn403

b:96.3
occ:1.00
SG B:CYS103 2.2 70.4 1.0
SG B:CYS111 2.2 69.9 1.0
SG B:CYS100 2.2 70.7 1.0
SG B:CYS97 2.2 72.0 1.0
CB B:CYS100 3.2 70.7 1.0
CB B:CYS111 3.3 69.9 1.0
CB B:CYS103 3.4 70.4 1.0
CB B:CYS97 3.5 72.0 1.0
N B:CYS97 3.5 72.0 1.0
N B:CYS100 4.0 70.7 1.0
CA B:CYS97 4.0 72.0 1.0
N B:GLY98 4.0 72.5 1.0
CA B:CYS111 4.0 69.9 1.0
CA B:CYS100 4.2 70.7 1.0
N B:LEU112 4.3 71.7 1.0
N B:CYS103 4.4 70.4 1.0
C B:CYS97 4.5 72.0 1.0
NZ B:LYS113 4.5 73.9 1.0
CA B:CYS103 4.5 70.4 1.0
C B:GLN96 4.6 68.5 1.0
C B:CYS111 4.6 69.9 1.0
N B:LYS99 4.8 72.4 1.0
CA B:GLN96 4.8 68.5 1.0
C B:CYS100 5.0 70.7 1.0

Reference:

M.A.Herzik Jr., M.Wu, G.C.Lander. High-Resolution Structure Determination of Sub-100 kDa Complexes Using Conventional Cryo-Em. Nat Commun V. 10 1032 2019.
ISSN: ESSN 2041-1723
PubMed: 30833564
DOI: 10.1038/S41467-019-08991-8
Page generated: Wed Dec 16 12:22:09 2020

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