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Mercury in PDB 1dlq: Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury

Enzymatic activity of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury

All present enzymatic activity of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury:
1.13.11.1;

Protein crystallography data

The structure of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury, PDB code: 1dlq was solved by M.W.Vetting, D.H.Ohlendorf, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 52.700, 87.600, 84.000, 90.00, 96.50, 90.00
R / Rfree (%) 18.8 / 22.4

Other elements in 1dlq:

The structure of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Mercury Binding Sites:

The binding sites of Mercury atom in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury (pdb code 1dlq). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 6 binding sites of Mercury where determined in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury, PDB code: 1dlq:
Jump to Mercury binding site number: 1; 2; 3; 4; 5; 6;

Mercury binding site 1 out of 6 in 1dlq

Go back to Mercury Binding Sites List in 1dlq
Mercury binding site 1 out of 6 in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg401

b:27.9
occ:0.65
SG A:CYS202 2.3 30.8 1.0
O A:HOH505 2.5 14.8 1.0
O A:GLY219 2.6 16.2 1.0
N A:CYS202 2.9 24.9 1.0
CA A:CYS202 3.1 25.9 1.0
CB A:CYS202 3.2 26.4 1.0
CE1 A:PHE253 3.4 14.9 1.0
CZ A:PHE253 3.4 14.6 1.0
C A:GLY201 3.4 24.5 1.0
C A:GLY219 3.6 16.0 1.0
CD1 A:PHE253 3.9 15.8 1.0
CE2 A:PHE253 3.9 15.7 1.0
CA A:GLY219 4.0 15.9 1.0
CA A:GLY201 4.0 24.3 1.0
O A:GLY201 4.0 24.4 1.0
CD1 A:LEU73 4.2 15.6 1.0
CD2 A:PHE253 4.3 15.8 1.0
CG A:PHE253 4.3 16.3 1.0
HG A:HG402 4.5 31.4 0.3
CG A:LEU73 4.5 15.7 1.0
CD2 A:LEU73 4.6 16.2 1.0
C A:CYS202 4.7 25.7 1.0
N A:ASN220 4.7 16.9 1.0
O A:TYR200 5.0 24.1 1.0

Mercury binding site 2 out of 6 in 1dlq

Go back to Mercury Binding Sites List in 1dlq
Mercury binding site 2 out of 6 in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg402

b:31.4
occ:0.35
N A:CYS202 2.4 24.9 1.0
OE1 A:GLN209 2.4 29.8 1.0
O A:CYS202 2.7 25.6 1.0
CB A:CYS202 2.8 26.4 1.0
CA A:CYS202 2.9 25.9 1.0
C A:CYS202 3.1 25.7 1.0
C A:GLY201 3.3 24.5 1.0
CD A:GLN209 3.6 28.5 1.0
CA A:GLY201 3.7 24.3 1.0
SG A:CYS202 3.8 30.8 1.0
O A:GLY219 3.9 16.2 1.0
CA A:GLY219 4.2 15.9 1.0
C A:GLY219 4.2 16.0 1.0
CG A:GLN209 4.3 26.8 1.0
O A:GLY201 4.4 24.4 1.0
N A:PRO203 4.4 26.0 1.0
CB A:GLN209 4.5 24.9 1.0
N A:GLY219 4.5 16.1 1.0
HG A:HG401 4.5 27.9 0.7
NE2 A:GLN209 4.6 28.6 1.0
N A:PRO204 4.7 28.6 1.0
C A:PRO203 4.7 27.3 1.0
OD1 A:ASN220 4.8 21.3 1.0
O A:PRO203 4.8 26.8 1.0
CA A:PRO204 4.8 29.6 1.0
N A:GLY201 5.0 23.9 1.0

Mercury binding site 3 out of 6 in 1dlq

Go back to Mercury Binding Sites List in 1dlq
Mercury binding site 3 out of 6 in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg403

b:26.9
occ:0.65
NE2 A:HIS82 2.3 11.7 1.0
SD A:MET86 2.9 25.8 1.0
CD2 A:HIS82 3.2 10.9 1.0
CE1 A:HIS82 3.3 11.4 1.0
CG A:MET86 3.6 21.1 1.0
CE A:MET86 4.1 23.0 1.0
CG A:HIS82 4.4 12.5 1.0
ND1 A:HIS82 4.4 12.7 1.0

Mercury binding site 4 out of 6 in 1dlq

Go back to Mercury Binding Sites List in 1dlq
Mercury binding site 4 out of 6 in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 4 of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg401

b:28.3
occ:0.65
SG B:CYS202 2.3 28.9 1.0
O B:HOH513 2.7 18.0 1.0
O B:GLY219 2.8 19.6 1.0
N B:CYS202 3.1 26.3 1.0
CZ B:PHE253 3.1 15.2 1.0
CA B:CYS202 3.2 27.4 1.0
CE1 B:PHE253 3.3 16.8 1.0
CB B:CYS202 3.3 27.2 1.0
C B:GLY201 3.6 25.4 1.0
CE2 B:PHE253 3.6 16.1 1.0
C B:GLY219 3.7 18.4 1.0
CD1 B:PHE253 3.8 17.0 1.0
CA B:GLY219 4.0 17.9 1.0
CD1 B:LEU73 4.1 14.1 1.0
CD2 B:PHE253 4.1 16.4 1.0
O B:GLY201 4.1 25.2 1.0
CA B:GLY201 4.2 25.5 1.0
CG B:PHE253 4.2 16.8 1.0
CG B:LEU73 4.4 13.3 1.0
CD2 B:LEU73 4.4 13.6 1.0
HG B:HG402 4.5 27.0 0.3
C B:CYS202 4.7 27.6 1.0
N B:ASN220 4.8 18.6 1.0

Mercury binding site 5 out of 6 in 1dlq

Go back to Mercury Binding Sites List in 1dlq
Mercury binding site 5 out of 6 in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 5 of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg402

b:27.0
occ:0.35
NE2 B:GLN209 2.2 30.0 1.0
N B:CYS202 2.3 26.3 1.0
CB B:CYS202 2.8 27.2 1.0
O B:CYS202 2.8 27.8 1.0
CA B:CYS202 2.8 27.4 1.0
C B:CYS202 3.1 27.6 1.0
C B:GLY201 3.3 25.4 1.0
CD B:GLN209 3.4 28.5 1.0
O B:GLY219 3.7 19.6 1.0
CA B:GLY201 3.7 25.5 1.0
SG B:CYS202 3.7 28.9 1.0
C B:GLY219 4.1 18.4 1.0
CA B:GLY219 4.1 17.9 1.0
OE1 B:GLN209 4.2 29.4 1.0
CG B:GLN209 4.2 26.6 1.0
O B:GLY201 4.3 25.2 1.0
N B:PRO203 4.4 28.1 1.0
HG B:HG401 4.5 28.3 0.7
N B:GLY219 4.5 17.7 1.0
CB B:GLN209 4.5 24.3 1.0
OD1 B:ASN220 4.7 22.3 1.0
C B:PRO203 4.8 28.6 1.0
O B:PRO203 4.8 29.1 1.0
N B:PRO204 4.8 29.3 1.0

Mercury binding site 6 out of 6 in 1dlq

Go back to Mercury Binding Sites List in 1dlq
Mercury binding site 6 out of 6 in the Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 6 of Structure of Catechol 1,2-Dioxygenase From Acinetobacter Sp. ADP1 Inhibited By Bound Mercury within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg403

b:23.6
occ:0.65
NE2 B:HIS82 2.1 16.0 1.0
SD B:MET86 3.0 24.1 1.0
CE1 B:HIS82 3.0 15.6 1.0
CD2 B:HIS82 3.2 14.8 1.0
CE B:MET86 3.5 23.3 1.0
CG B:MET86 3.8 19.9 1.0
ND1 B:HIS82 4.2 16.0 1.0
CG B:HIS82 4.3 15.6 1.0

Reference:

M.W.Vetting, D.H.Ohlendorf. The 1.8 A Crystal Structure of Catechol 1,2-Dioxygenase Reveals A Novel Hydrophobic Helical Zipper As A Subunit Linker. Structure Fold.Des. V. 8 429 2000.
ISSN: ISSN 0969-2126
PubMed: 10801478
DOI: 10.1016/S0969-2126(00)00122-2
Page generated: Wed Oct 28 18:39:07 2020

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