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Mercury in PDB 1ope: Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart

Enzymatic activity of Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart

All present enzymatic activity of Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart:
2.8.3.5;

Protein crystallography data

The structure of Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart, PDB code: 1ope was solved by A.M.Coros, L.Swenson, W.T.Wolodko, M.E.Fraser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.13 / 2.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 147.640, 68.700, 103.500, 90.00, 99.58, 90.00
R / Rfree (%) 18 / 23.5

Other elements in 1ope:

The structure of Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart also contains other interesting chemical elements:

Potassium (K) 2 atoms

Mercury Binding Sites:

The binding sites of Mercury atom in the Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart (pdb code 1ope). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 4 binding sites of Mercury where determined in the Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart, PDB code: 1ope:
Jump to Mercury binding site number: 1; 2; 3; 4;

Mercury binding site 1 out of 4 in 1ope

Go back to Mercury Binding Sites List in 1ope
Mercury binding site 1 out of 4 in the Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg482

b:43.1
occ:0.30
NE2 A:HIS157 2.4 29.3 1.0
O A:HOH519 2.5 32.6 1.0
CE1 A:HIS157 3.1 28.1 1.0
CD2 A:HIS157 3.5 25.8 1.0
ND1 A:HIS157 4.3 28.9 1.0
OH A:TYR122 4.4 21.2 1.0
CG A:HIS157 4.5 26.2 1.0

Mercury binding site 2 out of 4 in 1ope

Go back to Mercury Binding Sites List in 1ope
Mercury binding site 2 out of 4 in the Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg483

b:49.0
occ:0.30
NE2 A:HIS411 2.5 73.0 1.0
CD2 A:HIS411 3.3 72.5 1.0
CE1 A:HIS411 3.5 73.1 1.0
O A:LYS461 4.2 46.0 1.0
CG A:HIS411 4.5 72.2 1.0
ND1 A:HIS411 4.5 72.5 1.0

Mercury binding site 3 out of 4 in 1ope

Go back to Mercury Binding Sites List in 1ope
Mercury binding site 3 out of 4 in the Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg482

b:59.5
occ:0.30
NE2 B:HIS411 2.3 66.0 1.0
CE1 B:HIS411 3.0 65.5 1.0
CD2 B:HIS411 3.4 64.9 1.0
O B:LYS461 3.6 56.8 1.0
ND1 B:HIS411 4.1 64.9 1.0
CG B:HIS411 4.3 63.6 1.0
C B:LYS461 4.8 56.5 1.0

Mercury binding site 4 out of 4 in 1ope

Go back to Mercury Binding Sites List in 1ope
Mercury binding site 4 out of 4 in the Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 4 of Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg483

b:46.5
occ:0.30
NE2 B:HIS157 2.3 28.8 1.0
CD2 B:HIS157 3.3 25.9 1.0
CE1 B:HIS157 3.3 28.6 1.0
ND1 B:HIS157 4.4 26.5 1.0
CG B:HIS157 4.4 26.9 1.0
OH B:TYR122 4.6 23.7 1.0

Reference:

A.M.Coros, L.Swenson, W.T.Wolodko, M.E.Fraser. Structure of the Coa Transferase From Pig Heart to 1.7 A Resolution. Acta Crystallogr.,Sect.D V. 60 1717 2004.
ISSN: ISSN 0907-4449
PubMed: 15388917
DOI: 10.1107/S0907444904017974
Page generated: Sun Dec 13 19:04:34 2020

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