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Zinc in PDB 8zj0: Terephthalate 1,2-Cis-Dihydrodioldehydrogenase/Decarboxylase in Complex with 3-Hydroxybenzoate.

Enzymatic activity of Terephthalate 1,2-Cis-Dihydrodioldehydrogenase/Decarboxylase in Complex with 3-Hydroxybenzoate.

All present enzymatic activity of Terephthalate 1,2-Cis-Dihydrodioldehydrogenase/Decarboxylase in Complex with 3-Hydroxybenzoate.:
1.1.1.262;

Protein crystallography data

The structure of Terephthalate 1,2-Cis-Dihydrodioldehydrogenase/Decarboxylase in Complex with 3-Hydroxybenzoate., PDB code: 8zj0 was solved by K.A.Kumar, D.Pahwa, P.Kumar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.43 / 2.90
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 86.734, 94.273, 166.395, 90, 90, 90
R / Rfree (%) 24.9 / 28.2

Other elements in 8zj0:

The structure of Terephthalate 1,2-Cis-Dihydrodioldehydrogenase/Decarboxylase in Complex with 3-Hydroxybenzoate. also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Terephthalate 1,2-Cis-Dihydrodioldehydrogenase/Decarboxylase in Complex with 3-Hydroxybenzoate. (pdb code 8zj0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Terephthalate 1,2-Cis-Dihydrodioldehydrogenase/Decarboxylase in Complex with 3-Hydroxybenzoate., PDB code: 8zj0:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 8zj0

Go back to Zinc Binding Sites List in 8zj0
Zinc binding site 1 out of 4 in the Terephthalate 1,2-Cis-Dihydrodioldehydrogenase/Decarboxylase in Complex with 3-Hydroxybenzoate.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Terephthalate 1,2-Cis-Dihydrodioldehydrogenase/Decarboxylase in Complex with 3-Hydroxybenzoate. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn401

b:5.0
occ:1.00
 NE2 B:HIS159 2.2 0.5 1.0
NE2 C:HIS203 2.3 0.5 1.0
NE2 B:HIS255 2.4 0.5 1.0
NE2 B:HIS259 3.0 0.5 1.0
CE1 B:HIS159 3.1 0.5 1.0
CE1 C:HIS203 3.2 0.5 1.0
CD2 B:HIS159 3.2 0.5 1.0
HE1 C:HIS203 3.3 0.5 1.0
HE1 B:HIS159 3.3 0.5 1.0
CE1 B:HIS255 3.3 0.5 1.0
HD2 B:HIS159 3.4 0.5 1.0
CD2 C:HIS203 3.4 0.5 1.0
CD2 B:HIS255 3.4 0.5 1.0
HD2 B:HIS259 3.4 0.5 1.0
HE1 B:HIS255 3.4 0.5 1.0
HD2 B:HIS255 3.5 0.5 1.0
CD2 B:HIS259 3.6 0.5 1.0
HD2 C:HIS203 3.6 0.5 1.0
CE1 B:HIS259 4.1 0.5 1.0
ND1 B:HIS159 4.3 0.5 1.0
ND1 C:HIS203 4.3 0.5 1.0
CG B:HIS159 4.3 0.5 1.0
HE1 B:HIS259 4.4 0.5 1.0
CG C:HIS203 4.5 0.5 1.0
ND1 B:HIS255 4.5 0.5 1.0
CG B:HIS255 4.5 0.5 1.0
HD12 B:LEU158 4.8 0.5 1.0
CG B:HIS259 4.8 0.5 1.0

Zinc binding site 2 out of 4 in 8zj0

Go back to Zinc Binding Sites List in 8zj0
Zinc binding site 2 out of 4 in the Terephthalate 1,2-Cis-Dihydrodioldehydrogenase/Decarboxylase in Complex with 3-Hydroxybenzoate.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Terephthalate 1,2-Cis-Dihydrodioldehydrogenase/Decarboxylase in Complex with 3-Hydroxybenzoate. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn401

b:4.5
occ:1.00
 NE2 C:HIS255 2.3 0.5 1.0
NE2 C:HIS159 2.4 0.5 1.0
NE2 B:HIS203 2.5 0.5 1.0
HE1 C:HIS159 2.7 0.5 1.0
NE2 C:HIS259 2.7 0.5 1.0
CE1 C:HIS159 2.8 0.5 1.0
CD2 C:HIS255 3.2 0.5 1.0
CE1 B:HIS203 3.3 0.5 1.0
CE1 C:HIS255 3.3 0.5 1.0
HD2 C:HIS259 3.3 0.5 1.0
HE1 B:HIS203 3.3 0.5 1.0
HD2 C:HIS255 3.4 0.5 1.0
CD2 C:HIS259 3.4 0.5 1.0
HE1 C:HIS255 3.5 0.5 1.0
CD2 B:HIS203 3.5 0.5 1.0
CD2 C:HIS159 3.6 0.5 1.0
HD2 B:HIS203 3.8 0.5 1.0
CE1 C:HIS259 3.8 0.5 1.0
ND1 C:HIS159 4.0 0.5 1.0
HD2 C:HIS159 4.1 0.5 1.0
HE1 C:HIS259 4.2 0.5 1.0
ND1 C:HIS255 4.4 0.5 1.0
CG C:HIS255 4.4 0.5 1.0
HD1 C:HIS159 4.5 30.0 0.0
ND1 B:HIS203 4.5 0.5 1.0
CG C:HIS159 4.5 0.5 1.0
HD12 C:LEU158 4.5 0.5 1.0
CG C:HIS259 4.6 0.5 1.0
CG B:HIS203 4.6 0.5 1.0
ND1 C:HIS259 4.8 0.5 1.0
HG C:LEU158 4.8 0.5 1.0
HE3 C:LYS263 4.9 0.5 1.0

Zinc binding site 3 out of 4 in 8zj0

Go back to Zinc Binding Sites List in 8zj0
Zinc binding site 3 out of 4 in the Terephthalate 1,2-Cis-Dihydrodioldehydrogenase/Decarboxylase in Complex with 3-Hydroxybenzoate.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Terephthalate 1,2-Cis-Dihydrodioldehydrogenase/Decarboxylase in Complex with 3-Hydroxybenzoate. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn402

b:4.6
occ:1.00
 NE2 D:HIS203 2.2 0.5 1.0
CE1 D:HIS203 3.1 0.5 1.0
CD2 D:HIS203 3.1 0.5 1.0
HE1 D:HIS203 3.2 0.5 1.0
HD2 D:HIS203 3.3 0.5 1.0
ND1 D:HIS203 4.2 0.5 1.0
CG D:HIS203 4.2 0.5 1.0
HB3 D:PRO202 4.8 0.5 1.0
HD1 D:HIS203 4.9 30.0 0.0

Zinc binding site 4 out of 4 in 8zj0

Go back to Zinc Binding Sites List in 8zj0
Zinc binding site 4 out of 4 in the Terephthalate 1,2-Cis-Dihydrodioldehydrogenase/Decarboxylase in Complex with 3-Hydroxybenzoate.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Terephthalate 1,2-Cis-Dihydrodioldehydrogenase/Decarboxylase in Complex with 3-Hydroxybenzoate. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn403

b:3.8
occ:1.00
 NE2 D:HIS159 1.9 0.5 1.0
O1' D:3HB401 2.0 1.3 1.0
NE2 D:HIS255 2.1 0.5 1.0
O2' D:3HB401 2.4 1.1 1.0
C1' D:3HB401 2.4 1.2 1.0
CE1 D:HIS159 2.8 0.5 1.0
HE1 D:HIS159 2.9 0.5 1.0
CD2 D:HIS159 3.0 0.5 1.0
NE2 D:HIS259 3.1 0.5 1.0
CD2 D:HIS255 3.1 0.5 1.0
CE1 D:HIS255 3.1 0.5 1.0
HD2 D:HIS159 3.2 0.5 1.0
HD2 D:HIS255 3.3 0.5 1.0
HE1 D:HIS255 3.3 0.5 1.0
HD2 D:HIS259 3.5 0.5 1.0
CD2 D:HIS259 3.6 0.5 1.0
C1 D:3HB401 3.9 1.2 1.0
ND1 D:HIS159 3.9 0.5 1.0
CG D:HIS159 4.0 0.5 1.0
CE1 D:HIS259 4.2 0.5 1.0
ND1 D:HIS255 4.2 0.5 1.0
CG D:HIS255 4.2 0.5 1.0
H2 D:3HB401 4.4 1.1 1.0
HE1 D:HIS259 4.5 0.5 1.0
C2 D:3HB401 4.6 1.1 1.0
HD12 D:LEU158 4.7 0.5 1.0
HD1 D:HIS159 4.7 30.0 0.0
H6 D:3HB401 4.7 1.1 1.0
HG D:LEU158 4.8 0.5 1.0
C6 D:3HB401 4.8 1.1 1.0
CG D:HIS259 4.8 0.5 1.0

Reference:

K.A.Kumar, D.Pahwa. Terephthalate 1,2-Cis-Dihydrodioldehydrogenase/Decarboxylase in Complex with 3-Hydroxybenzoate. To Be Published.
Page generated: Fri Aug 22 16:13:59 2025

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