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Mercury in PDB 2di4: Crystal Structure of the Ftsh Protease Domain

Protein crystallography data

The structure of Crystal Structure of the Ftsh Protease Domain, PDB code: 2di4 was solved by R.Suno, H.Niwa, D.Tsuchiya, X.Zhang, M.Yoshida, K.Morikawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.79
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 116.800, 116.800, 63.500, 90.00, 90.00, 120.00
R / Rfree (%) 25.1 / 29.9

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of the Ftsh Protease Domain (pdb code 2di4). 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 Protease Domain, PDB code: 2di4:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in 2di4

Go back to Mercury Binding Sites List in 2di4
Mercury binding site 1 out of 2 in the Crystal Structure of the Ftsh Protease Domain


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 Protease Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg1001

b:25.3
occ:0.20
OD2 A:ASP496 1.9 45.4 1.0
NE2 A:HIS418 2.0 39.6 1.0
NE2 A:HIS422 2.2 40.0 1.0
CG A:ASP496 2.9 46.1 1.0
CD2 A:HIS418 2.9 41.0 1.0
CE1 A:HIS418 3.0 40.9 1.0
CE1 A:HIS422 3.1 40.8 1.0
CD2 A:HIS422 3.1 41.8 1.0
OD1 A:ASP496 3.1 47.5 1.0
CG A:HIS418 4.1 41.3 1.0
ND1 A:HIS418 4.1 39.8 1.0
ND1 A:HIS422 4.2 41.6 1.0
CG A:HIS422 4.2 41.0 1.0
OE2 A:GLU419 4.3 48.2 1.0
CB A:ASP496 4.3 44.0 1.0
O A:GLY492 4.4 40.1 1.0
O A:HOH10 4.4 25.9 1.0
O A:HOH2 4.7 30.6 1.0

Mercury binding site 2 out of 2 in 2di4

Go back to Mercury Binding Sites List in 2di4
Mercury binding site 2 out of 2 in the Crystal Structure of the Ftsh Protease Domain


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 Protease Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg2001

b:92.3
occ:1.00
OD2 B:ASP496 2.2 49.4 1.0
NE2 B:HIS418 2.3 43.3 1.0
NE2 B:HIS422 2.4 40.8 1.0
CG B:ASP496 3.0 46.3 1.0
CD2 B:HIS418 3.1 42.9 1.0
CD2 B:HIS422 3.3 40.5 1.0
OD1 B:ASP496 3.3 47.5 1.0
CE1 B:HIS422 3.4 42.1 1.0
CE1 B:HIS418 3.5 43.6 1.0
OE1 B:GLU419 4.0 41.7 1.0
O B:GLY492 4.3 41.9 1.0
CG B:HIS418 4.3 43.0 1.0
CB B:ASP496 4.4 43.9 1.0
CG B:HIS422 4.4 40.5 1.0
ND1 B:HIS422 4.4 41.8 1.0
ND1 B:HIS418 4.5 43.9 1.0
CA B:GLY476 5.0 39.9 1.0

Reference:

R.Suno, H.Niwa, D.Tsuchiya, X.Zhang, M.Yoshida, K.Morikawa. Structure of the Whole Cytosolic Region of Atp-Dependent Protease Ftsh Mol.Cell V. 22 575 2006.
ISSN: ISSN 1097-2765
PubMed: 16762831
DOI: 10.1016/J.MOLCEL.2006.04.020
Page generated: Wed Oct 28 18:41:20 2020

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