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Zinc in PDB 2o03: Crystal Structure of Furb From M. Tuberculosis- A Zinc Uptake Regulator

Protein crystallography data

The structure of Crystal Structure of Furb From M. Tuberculosis- A Zinc Uptake Regulator, PDB code: 2o03 was solved by D.Lucarelli, S.Russo, E.Pohl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.69 / 2.70
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 51.600, 51.600, 133.400, 90.00, 90.00, 90.00
R / Rfree (%) 23 / 23.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Furb From M. Tuberculosis- A Zinc Uptake Regulator (pdb code 2o03). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of Furb From M. Tuberculosis- A Zinc Uptake Regulator, PDB code: 2o03:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 2o03

Go back to Zinc Binding Sites List in 2o03
Zinc binding site 1 out of 3 in the Crystal Structure of Furb From M. Tuberculosis- A Zinc Uptake Regulator


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Furb From M. Tuberculosis- A Zinc Uptake Regulator within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:62.1
occ:1.00
OD2 A:ASP62 2.0 56.3 1.0
NE2 A:HIS83 2.0 55.0 1.0
NE2 A:HIS81 2.1 55.1 1.0
SG A:CYS76 2.3 51.0 1.0
CD2 A:HIS83 2.8 51.1 1.0
CG A:ASP62 2.8 52.5 1.0
OD1 A:ASP62 3.0 52.1 1.0
CE1 A:HIS81 3.0 53.0 1.0
CD2 A:HIS81 3.2 52.1 1.0
CE1 A:HIS83 3.2 52.0 1.0
CB A:CYS76 3.8 51.5 1.0
CG A:HIS83 4.0 49.9 1.0
ND1 A:HIS83 4.2 52.1 1.0
ND1 A:HIS81 4.2 52.3 1.0
CA A:CYS76 4.2 52.0 1.0
CB A:ASP62 4.2 51.9 1.0
CG A:HIS81 4.3 51.2 1.0
N A:SER77 4.3 53.2 1.0
CB A:GLU94 4.8 51.1 1.0
C A:CYS76 4.8 52.6 1.0
OE1 A:GLU94 4.9 51.1 1.0
CG A:GLU94 5.0 51.1 1.0

Zinc binding site 2 out of 3 in 2o03

Go back to Zinc Binding Sites List in 2o03
Zinc binding site 2 out of 3 in the Crystal Structure of Furb From M. Tuberculosis- A Zinc Uptake Regulator


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Furb From M. Tuberculosis- A Zinc Uptake Regulator within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn202

b:67.5
occ:1.00
SG A:CYS86 2.3 53.3 1.0
SG A:CYS89 2.4 52.5 1.0
SG A:CYS129 2.4 61.9 1.0
SG A:CYS126 2.4 56.5 1.0
CB A:CYS129 3.1 63.3 1.0
CB A:CYS86 3.2 51.6 1.0
CB A:CYS126 3.4 56.0 1.0
CB A:CYS89 3.5 53.2 1.0
N A:CYS89 3.8 52.5 1.0
N A:CYS126 4.1 55.3 1.0
CA A:CYS129 4.2 63.4 1.0
CA A:CYS126 4.2 56.3 1.0
N A:CYS129 4.2 62.8 1.0
CA A:CYS89 4.3 53.1 1.0
CB A:SER88 4.3 50.8 1.0
C A:SER88 4.6 51.8 1.0
CA A:CYS86 4.6 51.8 1.0
CB A:SER91 4.8 54.0 1.0
N A:SER88 4.8 51.4 1.0
CA A:SER88 4.8 51.3 1.0
C A:CYS126 4.8 56.9 1.0

Zinc binding site 3 out of 3 in 2o03

Go back to Zinc Binding Sites List in 2o03
Zinc binding site 3 out of 3 in the Crystal Structure of Furb From M. Tuberculosis- A Zinc Uptake Regulator


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Furb From M. Tuberculosis- A Zinc Uptake Regulator within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn203

b:47.3
occ:0.50
OE1 A:GLU101 2.0 53.2 1.0
NE2 A:HIS82 2.1 48.6 1.0
NE2 A:HIS80 2.1 45.2 1.0
NE2 A:HIS118 2.1 54.7 1.0
OE2 A:GLU101 2.4 58.4 1.0
CD A:GLU101 2.5 56.6 1.0
CE1 A:HIS118 2.8 55.7 1.0
CE1 A:HIS82 2.9 49.1 1.0
CD2 A:HIS80 3.0 46.0 1.0
CD2 A:HIS82 3.1 48.6 1.0
CE1 A:HIS80 3.1 46.2 1.0
CD2 A:HIS118 3.3 56.0 1.0
ND1 A:HIS82 4.0 49.2 1.0
CG A:GLU101 4.0 56.0 1.0
ND1 A:HIS118 4.1 55.4 1.0
CG A:HIS82 4.1 48.9 1.0
CG A:HIS80 4.2 47.5 1.0
ND1 A:HIS80 4.2 47.0 1.0
CG A:HIS118 4.3 55.3 1.0
CD1 A:ILE120 4.4 57.2 1.0
CB A:GLU101 4.8 55.9 1.0

Reference:

D.Lucarelli, S.Russo, E.Garman, A.Milano, W.Meyer-Klaucke, E.Pohl. Crystal Structure and Function of the Zinc Uptake Regulator Furb From Mycobacterium Tuberculosis. J.Biol.Chem. V. 282 9914 2007.
ISSN: ISSN 0021-9258
PubMed: 17213192
DOI: 10.1074/JBC.M609974200
Page generated: Wed Dec 16 03:45:07 2020

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