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Zinc in PDB 1teh: Structure of Human Liver Chichi Alcohol Dehydrogenase (A Glutathione- Dependent Formaldehyde Dehydrogenase)

Enzymatic activity of Structure of Human Liver Chichi Alcohol Dehydrogenase (A Glutathione- Dependent Formaldehyde Dehydrogenase)

All present enzymatic activity of Structure of Human Liver Chichi Alcohol Dehydrogenase (A Glutathione- Dependent Formaldehyde Dehydrogenase):
1.1.1.1; 1.2.1.1;

Protein crystallography data

The structure of Structure of Human Liver Chichi Alcohol Dehydrogenase (A Glutathione- Dependent Formaldehyde Dehydrogenase), PDB code: 1teh was solved by Z.-N.Yang, T.D.Hurley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.70
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 141.250, 201.550, 69.610, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 28.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Human Liver Chichi Alcohol Dehydrogenase (A Glutathione- Dependent Formaldehyde Dehydrogenase) (pdb code 1teh). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the Structure of Human Liver Chichi Alcohol Dehydrogenase (A Glutathione- Dependent Formaldehyde Dehydrogenase), PDB code: 1teh:
Jump to Zinc binding site number: 1; 2; 3; 4; 5;

Zinc binding site 1 out of 5 in 1teh

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Zinc binding site 1 out of 5 in the Structure of Human Liver Chichi Alcohol Dehydrogenase (A Glutathione- Dependent Formaldehyde Dehydrogenase)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Human Liver Chichi Alcohol Dehydrogenase (A Glutathione- Dependent Formaldehyde Dehydrogenase) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn375

b:28.7
occ:1.00
 SG A:CYS103 2.1 32.1 1.0
SG A:CYS97 2.2 35.3 1.0
SG A:CYS111 2.2 35.8 1.0
SG A:CYS100 2.3 33.0 1.0
CB A:CYS103 3.0 30.2 1.0
CB A:CYS111 3.1 30.0 1.0
CB A:CYS97 3.1 29.7 1.0
CB A:CYS100 3.3 28.4 1.0
N A:CYS97 3.5 26.5 1.0
CA A:CYS111 3.7 27.4 1.0
CA A:CYS97 3.8 23.2 1.0
N A:GLY98 3.8 20.1 1.0
N A:CYS100 3.9 32.4 1.0
N A:CYS103 4.1 33.5 1.0
CA A:CYS103 4.1 33.2 1.0
C A:CYS97 4.2 21.2 1.0
CA A:CYS100 4.2 30.1 1.0
N A:GLN112 4.4 36.8 1.0
C A:GLN96 4.4 23.6 1.0
C A:CYS111 4.4 33.0 1.0
N A:GLU99 4.5 29.8 1.0
CB A:LYS113 4.5 35.4 1.0
N A:LYS113 4.7 36.8 1.0
CA A:GLN96 4.7 17.9 1.0
CA A:GLY98 4.8 27.3 1.0
N A:CYS111 4.9 21.3 1.0
C A:CYS100 4.9 29.5 1.0

Zinc binding site 2 out of 5 in 1teh

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Zinc binding site 2 out of 5 in the Structure of Human Liver Chichi Alcohol Dehydrogenase (A Glutathione- Dependent Formaldehyde Dehydrogenase)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Human Liver Chichi Alcohol Dehydrogenase (A Glutathione- Dependent Formaldehyde Dehydrogenase) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn376

b:42.4
occ:1.00
 NE2 A:HIS67 2.1 30.3 1.0
SG A:CYS174 2.2 33.0 1.0
SG A:CYS46 2.3 32.4 1.0
CB A:CYS46 2.5 30.8 1.0
CE1 A:HIS67 2.7 28.8 1.0
OE2 A:GLU68 2.9 32.4 1.0
CD2 A:HIS67 3.1 26.1 1.0
CB A:CYS174 3.1 25.0 1.0
O A:HOH378 3.2 12.6 1.0
CD A:GLU68 3.4 30.1 1.0
CG A:GLU68 3.4 25.9 1.0
ND1 A:HIS67 3.8 31.1 1.0
CA A:CYS46 4.0 30.8 1.0
CG A:HIS67 4.0 26.9 1.0
NH2 A:ARG369 4.3 25.0 1.0
OE1 A:GLU68 4.4 31.6 1.0
CB A:THR48 4.6 36.6 1.0
CA A:CYS174 4.6 21.5 1.0
N A:CYS46 4.6 27.4 1.0
OG1 A:THR48 4.6 43.9 1.0
N A:GLY175 4.7 21.8 1.0
OD2 A:ASP49 4.8 38.4 1.0
CB A:GLU68 4.8 21.9 1.0
NE A:ARG369 4.9 21.6 1.0
C A:CYS46 4.9 32.1 1.0

Zinc binding site 3 out of 5 in 1teh

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Zinc binding site 3 out of 5 in the Structure of Human Liver Chichi Alcohol Dehydrogenase (A Glutathione- Dependent Formaldehyde Dehydrogenase)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure of Human Liver Chichi Alcohol Dehydrogenase (A Glutathione- Dependent Formaldehyde Dehydrogenase) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn375

b:46.5
occ:1.00
 SG B:CYS111 2.1 35.9 1.0
SG B:CYS103 2.1 37.6 1.0
SG B:CYS97 2.2 36.7 1.0
SG B:CYS100 2.3 42.6 1.0
CB B:CYS111 3.0 35.2 1.0
CB B:CYS97 3.0 31.1 1.0
CB B:CYS103 3.2 37.2 1.0
CB B:CYS100 3.3 37.5 1.0
N B:CYS97 3.5 24.9 1.0
N B:GLY98 3.6 25.2 1.0
CA B:CYS97 3.7 28.1 1.0
N B:CYS100 3.8 38.8 1.0
CA B:CYS111 3.8 29.9 1.0
C B:CYS97 4.0 25.8 1.0
CA B:CYS100 4.1 38.3 1.0
CB B:LYS113 4.2 35.7 1.0
N B:CYS103 4.2 33.9 1.0
CA B:CYS103 4.3 34.7 1.0
N B:GLU99 4.3 32.8 1.0
O B:CYS100 4.4 33.9 1.0
C B:GLN96 4.5 23.6 1.0
C B:CYS111 4.6 32.4 1.0
C B:CYS100 4.6 36.4 1.0
CA B:GLY98 4.7 26.2 1.0
N B:GLN112 4.7 35.3 1.0
N B:LYS113 4.7 37.8 1.0
O B:PRO95 4.9 35.9 1.0
C B:GLU99 4.9 37.4 1.0
CG B:LYS113 5.0 35.3 1.0

Zinc binding site 4 out of 5 in 1teh

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Zinc binding site 4 out of 5 in the Structure of Human Liver Chichi Alcohol Dehydrogenase (A Glutathione- Dependent Formaldehyde Dehydrogenase)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structure of Human Liver Chichi Alcohol Dehydrogenase (A Glutathione- Dependent Formaldehyde Dehydrogenase) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn376

b:35.9
occ:1.00
 NE2 B:HIS67 2.0 35.0 1.0
OE2 B:GLU68 2.0 26.4 1.0
SG B:CYS174 2.3 30.9 1.0
SG B:CYS46 2.3 29.1 1.0
CB B:CYS46 2.6 35.5 1.0
CE1 B:HIS67 2.9 35.3 1.0
CD B:GLU68 3.0 23.4 1.0
CD2 B:HIS67 3.1 36.6 1.0
CB B:CYS174 3.2 26.6 1.0
CG B:GLU68 3.3 20.9 1.0
NH2 B:ARG369 3.6 21.3 1.0
O B:HOH380 4.0 31.3 1.0
ND1 B:HIS67 4.0 39.1 1.0
CG B:HIS67 4.1 35.0 1.0
CA B:CYS46 4.1 33.6 1.0
OE1 B:GLU68 4.2 30.6 1.0
OG1 B:THR48 4.2 36.4 1.0
NE B:ARG369 4.4 21.1 1.0
CZ B:ARG369 4.4 22.4 1.0
CA B:CYS174 4.7 23.1 1.0
CB B:GLU68 4.7 24.5 1.0
CB B:THR48 4.7 36.5 1.0
N B:CYS46 4.8 31.3 1.0
N B:GLY175 4.8 23.7 1.0
OD2 B:ASP49 4.9 16.5 1.0
C B:CYS46 4.9 37.3 1.0

Zinc binding site 5 out of 5 in 1teh

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Zinc binding site 5 out of 5 in the Structure of Human Liver Chichi Alcohol Dehydrogenase (A Glutathione- Dependent Formaldehyde Dehydrogenase)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Structure of Human Liver Chichi Alcohol Dehydrogenase (A Glutathione- Dependent Formaldehyde Dehydrogenase) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn378

b:36.5
occ:0.50
 OE2 B:GLU360 1.9 21.2 1.0
ND1 B:HIS363 2.1 39.0 1.0
OE1 B:GLU360 2.3 28.6 1.0
CD B:GLU360 2.4 29.1 1.0
CG B:HIS363 3.0 35.2 1.0
CE1 B:HIS363 3.2 42.3 1.0
CB B:HIS363 3.2 32.6 1.0
CG B:GLU360 3.9 24.6 1.0
CD2 B:HIS363 4.2 38.4 1.0
NE2 B:HIS363 4.3 39.7 1.0
O B:GLU360 4.6 25.9 1.0
CA B:HIS363 4.7 33.6 1.0
CB B:GLU360 4.8 25.0 1.0
CA B:GLU360 4.8 25.5 1.0

Reference:

Z.N.Yang, W.F.Bosron, T.D.Hurley. Structure of Human Chi Chi Alcohol Dehydrogenase: A Glutathione-Dependent Formaldehyde Dehydrogenase. J.Mol.Biol. V. 265 330 1997.
ISSN: ISSN 0022-2836
PubMed: 9018047
DOI: 10.1006/JMBI.1996.0731
Page generated: Wed Oct 16 19:06:23 2024

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