Zinc in PDB 7luu: Kinetic and Structural Characterization of the First B3 Metallo-Beta- Lactamase with An Active Site Glutamic Acid

Protein crystallography data

The structure of Kinetic and Structural Characterization of the First B3 Metallo-Beta- Lactamase with An Active Site Glutamic Acid, PDB code: 7luu was solved by L.Wilson, E.Knaven, M.T.Morris, G.Schenk, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.19 / 1.68
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 62.64, 75.42, 56.67, 90, 90, 90
R / Rfree (%) 14.1 / 17

Zinc Binding Sites:

The binding sites of Zinc atom in the Kinetic and Structural Characterization of the First B3 Metallo-Beta- Lactamase with An Active Site Glutamic Acid (pdb code 7luu). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Kinetic and Structural Characterization of the First B3 Metallo-Beta- Lactamase with An Active Site Glutamic Acid, PDB code: 7luu:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 7luu

Go back to Zinc Binding Sites List in 7luu
Zinc binding site 1 out of 2 in the Kinetic and Structural Characterization of the First B3 Metallo-Beta- Lactamase with An Active Site Glutamic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Kinetic and Structural Characterization of the First B3 Metallo-Beta- Lactamase with An Active Site Glutamic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:17.5
occ:1.00
OE2 A:GLU102 1.9 16.4 1.0
O A:HOH444 1.9 20.0 1.0
NE2 A:HIS180 2.0 14.5 1.0
ND1 A:HIS104 2.0 16.5 1.0
CD2 A:HIS180 2.9 13.7 1.0
CD A:GLU102 2.9 15.5 1.0
CE1 A:HIS104 3.0 18.8 1.0
CG A:HIS104 3.0 14.5 1.0
CE1 A:HIS180 3.1 17.3 1.0
O3 A:GOL306 3.2 34.0 1.0
O A:HOH428 3.3 21.0 1.0
OE1 A:GLU102 3.4 15.5 1.0
CB A:HIS104 3.4 15.9 1.0
ZN A:ZN302 3.7 16.8 1.0
O2 A:GOL306 4.1 34.8 1.0
OE1 A:GLN143 4.1 29.3 1.0
CG A:HIS180 4.1 13.8 1.0
C3 A:GOL306 4.1 40.5 1.0
NE2 A:HIS104 4.1 18.1 1.0
OD1 A:ASP106 4.1 16.2 1.0
ND1 A:HIS180 4.1 15.0 1.0
CD2 A:HIS104 4.1 18.8 1.0
CD2 A:HIS107 4.3 15.5 1.0
CG A:GLU102 4.3 14.7 1.0
NE2 A:HIS107 4.4 13.1 1.0
O1 A:GOL306 4.5 20.2 1.0
C2 A:GOL306 4.6 40.9 1.0
C3 A:GOL308 4.7 40.9 1.0
O3 A:GOL308 4.8 44.7 1.0
OD2 A:ASP106 4.8 16.1 1.0
CA A:HIS104 4.9 12.3 1.0
CG A:ASP106 4.9 17.9 1.0

Zinc binding site 2 out of 2 in 7luu

Go back to Zinc Binding Sites List in 7luu
Zinc binding site 2 out of 2 in the Kinetic and Structural Characterization of the First B3 Metallo-Beta- Lactamase with An Active Site Glutamic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Kinetic and Structural Characterization of the First B3 Metallo-Beta- Lactamase with An Active Site Glutamic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:16.8
occ:1.00
NE2 A:HIS107 2.0 13.1 1.0
NE2 A:HIS247 2.0 15.9 1.0
O A:HOH428 2.1 21.0 1.0
OD2 A:ASP106 2.1 16.1 1.0
O2 A:GOL306 2.1 34.8 1.0
O A:HOH444 2.3 20.0 1.0
CD2 A:HIS107 3.0 15.5 1.0
CG A:ASP106 3.0 17.9 1.0
CE1 A:HIS107 3.0 15.2 1.0
CE1 A:HIS247 3.0 17.3 1.0
CD2 A:HIS247 3.0 17.3 1.0
OD1 A:ASP106 3.3 16.2 1.0
C2 A:GOL306 3.4 40.9 1.0
ZN A:ZN301 3.7 17.5 1.0
O1 A:GOL306 3.8 20.2 1.0
C1 A:GOL306 3.9 27.3 1.0
O3 A:GOL306 4.0 34.0 1.0
ND1 A:HIS107 4.1 15.6 1.0
CG A:HIS107 4.1 14.2 1.0
ND1 A:HIS247 4.1 19.1 1.0
CG A:HIS247 4.2 14.3 1.0
OE2 A:GLU102 4.2 16.4 1.0
OE1 A:GLU102 4.2 15.5 1.0
C3 A:GOL306 4.3 40.5 1.0
CB A:ASP106 4.4 16.8 1.0
CD A:GLU102 4.4 15.5 1.0
NE2 A:HIS180 4.8 14.5 1.0

Reference:

L.Wilson, E.Knaven, M.T.Morris, G.Schenk. Kinetic and Structural Characterization of the First B3 Metallo-Beta-Lactamase with An Active Site Glutamic Acid To Be Published.
Page generated: Sun Aug 22 09:48:09 2021

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