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Mercury in PDB 1z6a: Sulfolobus Solfataricus SWI2/SNF2 Atpase Core Domain

Protein crystallography data

The structure of Sulfolobus Solfataricus SWI2/SNF2 Atpase Core Domain, PDB code: 1z6a was solved by H.Duerr, C.Koerner, M.Mueller, V.Hickmann, K.P.Hopfner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 3.00
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 83.890, 83.890, 227.540, 90.00, 90.00, 90.00
R / Rfree (%) 24 / 29.7

Mercury Binding Sites:

The binding sites of Mercury atom in the Sulfolobus Solfataricus SWI2/SNF2 Atpase Core Domain (pdb code 1z6a). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 3 binding sites of Mercury where determined in the Sulfolobus Solfataricus SWI2/SNF2 Atpase Core Domain, PDB code: 1z6a:
Jump to Mercury binding site number: 1; 2; 3;

Mercury binding site 1 out of 3 in 1z6a

Go back to Mercury Binding Sites List in 1z6a
Mercury binding site 1 out of 3 in the Sulfolobus Solfataricus SWI2/SNF2 Atpase Core Domain


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Sulfolobus Solfataricus SWI2/SNF2 Atpase Core Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg951

b:0.5
occ:1.00
O A:CYS499 2.4 71.5 1.0
SG A:CYS499 2.5 77.2 1.0
C A:CYS499 3.2 72.1 1.0
O A:THR540 3.4 87.2 1.0
CB A:LEU504 3.5 76.3 1.0
CD1 A:LEU504 3.5 79.1 1.0
CB A:CYS499 3.6 73.5 1.0
C A:THR540 3.7 87.5 1.0
CA A:CYS499 3.7 73.2 1.0
N A:CYS499 3.8 72.9 1.0
CG A:LEU504 3.8 78.0 1.0
O A:PRO500 3.9 72.0 1.0
N A:THR540 3.9 86.4 1.0
C A:PRO500 4.0 72.6 1.0
CA A:LEU504 4.0 74.9 1.0
N A:PRO500 4.1 71.9 1.0
CA A:THR540 4.1 87.5 1.0
OG1 A:THR541 4.2 93.1 1.0
N A:THR541 4.2 88.2 1.0
N A:LEU501 4.3 73.5 1.0
N A:LEU504 4.4 73.4 1.0
CA A:LEU501 4.5 72.1 1.0
CA A:THR541 4.6 89.8 1.0
CA A:PRO500 4.6 71.9 1.0
CB A:LEU539 4.8 84.4 1.0
C A:LEU539 4.8 86.5 1.0
O A:LEU501 4.9 70.8 1.0

Mercury binding site 2 out of 3 in 1z6a

Go back to Mercury Binding Sites List in 1z6a
Mercury binding site 2 out of 3 in the Sulfolobus Solfataricus SWI2/SNF2 Atpase Core Domain


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Sulfolobus Solfataricus SWI2/SNF2 Atpase Core Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg952

b:0.6
occ:1.00
OG A:SER857 3.3 58.6 1.0
N A:LYS732 3.5 54.3 1.0
CB A:SER857 3.6 59.1 1.0
CB A:CYS670 3.7 64.3 1.0
CD2 A:LEU672 3.7 57.4 0.0
C A:GLY731 3.8 56.7 1.0
SG A:CYS670 3.8 68.3 1.0
CA A:GLY731 3.9 56.1 1.0
CG A:LYS732 3.9 51.8 1.0
O A:CYS670 4.0 63.0 1.0
C A:CYS670 4.1 61.4 1.0
CA A:SER857 4.2 60.9 1.0
CA A:LYS732 4.2 53.1 1.0
N A:LEU672 4.2 61.0 1.0
N A:GLY731 4.3 57.8 1.0
C A:ASN671 4.3 61.0 1.0
CG A:LEU672 4.3 56.9 1.0
O A:VAL714 4.4 60.3 1.0
CA A:LEU672 4.4 60.0 1.0
CB A:LYS732 4.5 51.1 1.0
O A:ASN671 4.5 60.3 1.0
N A:ASN671 4.5 62.1 1.0
CA A:CYS670 4.5 61.5 1.0
NE2 A:GLN676 4.5 69.7 1.0
O A:GLY731 4.6 58.1 1.0
CB A:VAL714 4.7 62.3 1.0
CA A:ASN671 4.8 62.1 1.0
CA A:VAL714 4.9 62.5 1.0
CB A:LEU672 4.9 57.1 1.0
C A:VAL714 5.0 60.4 1.0

Mercury binding site 3 out of 3 in 1z6a

Go back to Mercury Binding Sites List in 1z6a
Mercury binding site 3 out of 3 in the Sulfolobus Solfataricus SWI2/SNF2 Atpase Core Domain


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Sulfolobus Solfataricus SWI2/SNF2 Atpase Core Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg953

b:0.5
occ:1.00
SG A:CYS466 2.7 54.7 1.0
CB A:CYS466 3.6 59.0 1.0
CD1 A:LEU601 3.8 86.7 1.0
OG1 A:THR590 4.1 72.1 1.0
CD1 A:ILE646 4.1 50.1 1.0
CE A:LYS597 4.2 0.7 1.0
CD1 A:ILE604 4.2 72.8 1.0
CG2 A:ILE646 4.2 53.3 1.0
NZ A:LYS597 4.3 0.3 1.0
CG A:PRO593 4.3 0.8 1.0
CG1 A:ILE646 4.4 51.4 1.0
CG2 A:THR590 4.9 70.4 1.0
SD A:MET605 5.0 82.2 1.0

Reference:

H.Duerr, C.Koerner, M.Mueller, V.Hickmann, K.P.Hopfner. X-Ray Structures of the Sulfolobus Solfataricus SWI2/SNF2 Atpase Core and Its Complex with Dna Cell(Cambridge,Mass.) V. 121 363 2005.
ISSN: ISSN 0092-8674
PubMed: 15882619
DOI: 10.1016/J.CELL.2005.03.026
Page generated: Wed Oct 28 18:41:06 2020

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