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Mercury in PDB 1ixz: Crystal Structure of the Ftsh Atpase Domain From Thermus Thermophilus

Protein crystallography data

The structure of Crystal Structure of the Ftsh Atpase Domain From Thermus Thermophilus, PDB code: 1ixz was solved by H.Niwa, D.Tsuchiya, H.Makyio, M.Yoshida, K.Morikawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 12.00 / 2.20
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 73.535, 73.535, 88.468, 90.00, 90.00, 120.00
R / Rfree (%) 19.6 / 23.8

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of the Ftsh Atpase Domain From Thermus Thermophilus (pdb code 1ixz). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Crystal Structure of the Ftsh Atpase Domain From Thermus Thermophilus, PDB code: 1ixz:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in 1ixz

Go back to Mercury Binding Sites List in 1ixz
Mercury binding site 1 out of 2 in the Crystal Structure of the Ftsh Atpase Domain From Thermus Thermophilus


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystal Structure of the Ftsh Atpase Domain From Thermus Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg1

b:63.1
occ:0.20
O A:HOH465 2.6 34.6 1.0
NE2 A:HIS338 2.7 52.9 1.0
CE1 A:HIS338 3.6 50.1 1.0
CD2 A:HIS338 3.6 50.5 1.0
O A:HOH475 3.9 48.3 1.0
CG2 A:ILE334 4.1 35.5 1.0
ND1 A:HIS338 4.7 49.9 1.0
CG A:HIS338 4.8 48.4 1.0
CG1 A:ILE334 4.9 30.1 1.0
CB A:ILE334 5.0 31.0 1.0

Mercury binding site 2 out of 2 in 1ixz

Go back to Mercury Binding Sites List in 1ixz
Mercury binding site 2 out of 2 in the Crystal Structure of the Ftsh Atpase Domain From Thermus Thermophilus


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Crystal Structure of the Ftsh Atpase Domain From Thermus Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg2

b:56.1
occ:1.00
O A:HOH495 2.4 27.2 1.0
SG A:CYS250 2.6 39.1 1.0
O A:ALA244 2.8 30.2 1.0
O A:HIS247 3.0 39.6 1.0
CB A:CYS250 3.4 29.3 1.0
N A:CYS250 3.5 28.2 1.0
O A:ALA294 3.6 32.4 1.0
C A:HIS247 3.6 41.4 1.0
C A:ALA244 3.7 30.6 1.0
CA A:CYS250 3.9 30.1 1.0
CB A:ILE295 3.9 38.7 1.0
C A:PRO249 4.0 36.8 1.0
CA A:ALA248 4.1 42.4 1.0
N A:ALA248 4.1 41.0 1.0
CG1 A:ILE295 4.1 38.1 1.0
CA A:ILE295 4.3 35.8 1.0
C A:ALA294 4.3 34.3 1.0
CA A:PRO249 4.3 35.9 1.0
CB A:ALA244 4.4 28.2 1.0
C A:CYS250 4.4 29.5 1.0
CA A:ALA244 4.4 33.0 1.0
O A:CYS250 4.4 26.4 1.0
N A:LYS245 4.5 33.7 1.0
CA A:HIS247 4.5 41.5 1.0
CA A:LYS245 4.6 35.0 1.0
N A:HIS247 4.6 42.5 1.0
CD1 A:ILE295 4.6 43.0 1.0
N A:ILE295 4.6 35.0 1.0
O A:PRO249 4.7 35.9 1.0
CB A:HIS247 4.7 41.9 1.0
CB A:ALA248 4.9 41.5 1.0

Reference:

H.Niwa, D.Tsuchiya, H.Makyio, M.Yoshida, K.Morikawa. Hexameric Ring Structure of the Atpase Domain of the Membrane-Integrated Metalloprotease Ftsh From Thermus Thermophilus HB8 Structure V. 10 1415 2002.
ISSN: ISSN 0969-2126
PubMed: 12377127
DOI: 10.1016/S0969-2126(02)00855-9
Page generated: Sun Aug 11 00:17:40 2024

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