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Mercury in PDB 6brs: The Crystal Structure of the Ferredoxin Protease Fusc in Complex with Arabidopsis Ferredoxin, Ethylmercury Phosphate Soaked Dataset

Protein crystallography data

The structure of The Crystal Structure of the Ferredoxin Protease Fusc in Complex with Arabidopsis Ferredoxin, Ethylmercury Phosphate Soaked Dataset, PDB code: 6brs was solved by R.Grinter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.65 / 2.30
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 81.531, 127.369, 132.200, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 24.2

Mercury Binding Sites:

The binding sites of Mercury atom in the The Crystal Structure of the Ferredoxin Protease Fusc in Complex with Arabidopsis Ferredoxin, Ethylmercury Phosphate Soaked Dataset (pdb code 6brs). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 5 binding sites of Mercury where determined in the The Crystal Structure of the Ferredoxin Protease Fusc in Complex with Arabidopsis Ferredoxin, Ethylmercury Phosphate Soaked Dataset, PDB code: 6brs:
Jump to Mercury binding site number: 1; 2; 3; 4; 5;

Mercury binding site 1 out of 5 in 6brs

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Mercury binding site 1 out of 5 in the The Crystal Structure of the Ferredoxin Protease Fusc in Complex with Arabidopsis Ferredoxin, Ethylmercury Phosphate Soaked Dataset


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of The Crystal Structure of the Ferredoxin Protease Fusc in Complex with Arabidopsis Ferredoxin, Ethylmercury Phosphate Soaked Dataset within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg1004

b:75.5
occ:0.36
OE2 A:GLU165 2.1 93.5 1.0
NE2 A:HIS80 2.3 51.4 1.0
CD A:GLU165 2.8 95.5 1.0
CD2 A:HIS80 3.1 40.9 1.0
CE1 A:HIS80 3.3 40.8 1.0
CG A:GLU165 3.4 92.9 1.0
OE1 A:GLU165 3.7 91.3 1.0
NE2 A:HIS84 3.9 64.8 1.0
CG A:HIS80 4.3 47.5 1.0
ND1 A:HIS80 4.4 52.3 1.0
CD2 A:HIS84 4.6 60.5 1.0
OE2 A:GLU83 4.6 52.4 1.0
CB A:GLU165 4.7 89.1 1.0
OE1 A:GLU83 4.8 54.0 1.0
CE1 A:HIS84 4.9 67.3 1.0

Mercury binding site 2 out of 5 in 6brs

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Mercury binding site 2 out of 5 in the The Crystal Structure of the Ferredoxin Protease Fusc in Complex with Arabidopsis Ferredoxin, Ethylmercury Phosphate Soaked Dataset


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of The Crystal Structure of the Ferredoxin Protease Fusc in Complex with Arabidopsis Ferredoxin, Ethylmercury Phosphate Soaked Dataset within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg1005

b:66.4
occ:0.34
NE2 A:HIS147 2.4 53.5 1.0
CD2 A:HIS147 3.3 47.8 1.0
CE1 A:HIS147 3.5 55.6 1.0
CD2 A:LEU247 3.6 59.1 1.0
O A:TYR243 4.0 50.9 1.0
O A:HOH1210 4.2 46.5 1.0
CG A:LEU247 4.3 56.6 1.0
CG A:HIS147 4.5 51.2 1.0
ND1 A:HIS147 4.5 55.7 1.0
CB A:ALA246 4.8 41.9 1.0
N A:LEU247 4.8 63.5 1.0
C A:TYR243 4.9 49.9 1.0

Mercury binding site 3 out of 5 in 6brs

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Mercury binding site 3 out of 5 in the The Crystal Structure of the Ferredoxin Protease Fusc in Complex with Arabidopsis Ferredoxin, Ethylmercury Phosphate Soaked Dataset


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of The Crystal Structure of the Ferredoxin Protease Fusc in Complex with Arabidopsis Ferredoxin, Ethylmercury Phosphate Soaked Dataset within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg1006

b:56.9
occ:0.22
NZ A:LYS586 2.0 42.9 1.0
CE A:LYS586 2.5 43.0 1.0
O A:LEU593 2.7 33.6 1.0
CD2 A:LEU582 3.4 28.9 1.0
O A:ASN570 3.7 41.2 1.0
CD A:LYS586 3.9 41.1 1.0
C A:LEU593 3.9 31.7 1.0
O A:HOH1324 4.0 45.8 1.0
O A:HOH1107 4.0 36.0 1.0
CG A:LEU582 4.2 37.1 1.0
CD1 A:LEU582 4.3 26.2 1.0
OD1 A:ASN570 4.4 26.8 1.0
CA A:LEU593 4.7 31.3 1.0
CB A:LEU593 4.7 27.9 1.0
CD2 A:LEU619 4.8 22.9 1.0
N A:LEU593 4.8 38.4 1.0
N A:SER594 4.8 35.8 1.0
C A:ASN570 4.8 36.0 1.0
CG A:LYS586 5.0 41.5 1.0
CA A:SER594 5.0 36.3 1.0

Mercury binding site 4 out of 5 in 6brs

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Mercury binding site 4 out of 5 in the The Crystal Structure of the Ferredoxin Protease Fusc in Complex with Arabidopsis Ferredoxin, Ethylmercury Phosphate Soaked Dataset


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 4 of The Crystal Structure of the Ferredoxin Protease Fusc in Complex with Arabidopsis Ferredoxin, Ethylmercury Phosphate Soaked Dataset within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg1007

b:72.2
occ:0.46
ND1 A:HIS691 2.4 43.1 1.0
O A:HOH1270 3.2 35.3 1.0
CG A:HIS691 3.3 41.4 1.0
CE1 A:HIS691 3.3 34.6 1.0
CB A:HIS691 3.6 23.0 1.0
O A:ASN624 3.6 31.2 1.0
CA A:HIS691 3.8 34.7 1.0
O A:HIS691 3.9 31.2 1.0
CB A:ALA694 4.0 28.8 1.0
C A:HIS691 4.3 34.8 1.0
NE2 A:HIS691 4.5 47.8 1.0
CD2 A:HIS691 4.5 41.9 1.0
C A:ASN624 4.7 27.0 1.0
CA A:VAL625 4.9 25.1 1.0
C A:ALA694 5.0 34.2 1.0

Mercury binding site 5 out of 5 in 6brs

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Mercury binding site 5 out of 5 in the The Crystal Structure of the Ferredoxin Protease Fusc in Complex with Arabidopsis Ferredoxin, Ethylmercury Phosphate Soaked Dataset


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 5 of The Crystal Structure of the Ferredoxin Protease Fusc in Complex with Arabidopsis Ferredoxin, Ethylmercury Phosphate Soaked Dataset within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg1008

b:70.6
occ:0.18
ND1 A:HIS733 2.1 71.3 1.0
CG A:HIS733 2.9 76.2 1.0
CB A:HIS733 3.1 76.9 1.0
CE1 A:HIS733 3.2 74.0 1.0
CZ A:PHE665 3.6 47.5 1.0
CE1 A:PHE665 3.7 51.0 1.0
O A:HIS733 4.0 66.0 1.0
CD2 A:HIS733 4.1 76.9 1.0
NE2 A:HIS733 4.2 76.6 1.0
CE2 A:PHE665 4.2 38.7 1.0
CD1 A:PHE665 4.3 47.2 1.0
CA A:HIS733 4.3 75.1 1.0
C A:HIS733 4.4 66.5 1.0
CD2 A:PHE665 4.8 43.6 1.0
CG A:PHE665 4.8 42.1 1.0

Reference:

R.Grinter, I.D.Hay, J.Song, J.Wang, D.Teng, V.Dhanesakaran, J.J.Wilksch, M.R.Davies, D.Littler, S.A.Beckham, I.R.Henderson, R.A.Strugnell, G.Dougan, T.Lithgow. Fusc, A Member of the M16 Protease Family Acquired By Bacteria For Iron Piracy Against Plants. Plos Biol. V. 16 06026 2018.
ISSN: ESSN 1545-7885
PubMed: 30071011
DOI: 10.1371/JOURNAL.PBIO.2006026
Page generated: Sun Dec 13 19:13:31 2020

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