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Zinc in PDB 6u0z: Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with the Hydrolyzed Penicillin G

Enzymatic activity of Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with the Hydrolyzed Penicillin G

All present enzymatic activity of Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with the Hydrolyzed Penicillin G:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with the Hydrolyzed Penicillin G, PDB code: 6u0z was solved by Y.Kim, N.Maltseva, M.Endres, A.Joachimiak, Center For Structural Genomicsof Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.30 / 1.65
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 104.759, 104.759, 98.434, 90.00, 90.00, 120.00
R / Rfree (%) 15.8 / 18.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with the Hydrolyzed Penicillin G (pdb code 6u0z). 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 the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with the Hydrolyzed Penicillin G, PDB code: 6u0z:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 6u0z

Go back to Zinc Binding Sites List in 6u0z
Zinc binding site 1 out of 3 in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with the Hydrolyzed Penicillin G


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 the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with the Hydrolyzed Penicillin G within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn305

b:0.9
occ:0.50
 O A:HOH586 2.5 45.0 1.0
O A:HOH572 2.6 39.6 1.0
OD1 A:ASP49 4.4 21.9 1.0
CG A:ASP49 4.7 24.3 1.0
O A:HOH566 4.9 47.4 1.0

Zinc binding site 2 out of 3 in 6u0z

Go back to Zinc Binding Sites List in 6u0z
Zinc binding site 2 out of 3 in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with the Hydrolyzed Penicillin G


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 the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with the Hydrolyzed Penicillin G within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn307

b:16.1
occ:1.00
 O A:HOH401 1.8 23.2 1.0
NE2 A:HIS181 2.0 14.0 1.0
NE2 A:HIS105 2.0 14.7 1.0
ND1 A:HIS107 2.1 16.4 1.0
O4 A:PNK306 2.5 35.2 1.0
CD2 A:HIS181 2.9 13.7 1.0
CD2 A:HIS105 3.0 14.7 1.0
CE1 A:HIS105 3.0 14.6 1.0
CE1 A:HIS107 3.0 16.0 1.0
CE1 A:HIS181 3.1 15.5 1.0
CG A:HIS107 3.1 14.0 1.0
CB A:HIS107 3.4 14.7 1.0
O2 A:PNK306 3.6 25.0 1.0
ZN A:ZN308 3.7 15.7 0.7
C2 A:PNK306 3.7 49.4 1.0
N1 A:PNK306 3.9 54.2 1.0
ND1 A:HIS105 4.1 15.1 1.0
CG A:HIS105 4.1 12.7 1.0
CG A:HIS181 4.1 12.6 1.0
ND1 A:HIS181 4.1 13.5 1.0
NE2 A:HIS107 4.2 14.2 1.0
CD2 A:HIS110 4.2 16.9 1.0
C9 A:PNK306 4.2 40.6 1.0
C5 A:PNK306 4.2 49.8 1.0
OD1 A:ASP109 4.2 17.0 1.0
CD2 A:HIS107 4.2 17.1 1.0
NE2 A:HIS110 4.4 17.1 1.0
C1 A:PNK306 4.4 51.0 1.0
C4 A:PNK306 4.8 53.0 1.0
CA A:HIS107 4.9 13.6 1.0
OD2 A:ASP109 4.9 20.2 1.0

Zinc binding site 3 out of 3 in 6u0z

Go back to Zinc Binding Sites List in 6u0z
Zinc binding site 3 out of 3 in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with the Hydrolyzed Penicillin G


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 the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with the Hydrolyzed Penicillin G within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn308

b:15.7
occ:0.74
 NE2 A:HIS110 2.0 17.1 1.0
OD2 A:ASP109 2.1 20.2 1.0
NE2 A:HIS246 2.1 22.7 1.0
O2 A:PNK306 2.3 25.0 1.0
O A:HOH401 2.3 23.2 1.0
N1 A:PNK306 2.3 54.2 1.0
CG A:ASP109 2.9 17.0 1.0
CE1 A:HIS110 3.0 18.0 1.0
C9 A:PNK306 3.0 40.6 1.0
CD2 A:HIS110 3.0 16.9 1.0
CD2 A:HIS246 3.0 24.8 1.0
CE1 A:HIS246 3.1 22.6 1.0
C5 A:PNK306 3.1 49.8 1.0
OD1 A:ASP109 3.2 17.0 1.0
C4 A:PNK306 3.5 53.0 1.0
ZN A:ZN307 3.7 16.1 1.0
ND1 A:HIS110 4.1 14.6 1.0
CG A:HIS110 4.1 13.6 1.0
O4 A:PNK306 4.1 35.2 1.0
O1 A:PNK306 4.2 28.7 1.0
CG A:HIS246 4.2 16.1 1.0
ND1 A:HIS246 4.2 21.2 1.0
C1 A:PNK306 4.2 51.0 1.0
NE2 A:HIS105 4.2 14.7 1.0
CE1 A:HIS105 4.2 14.6 1.0
C6 A:PNK306 4.3 46.9 1.0
CB A:ASP109 4.3 13.6 1.0
C13 A:PNK306 4.4 44.3 1.0
OG A:SER206 4.6 19.0 1.0
C2 A:PNK306 4.6 49.4 1.0
S1 A:PNK306 4.8 51.9 1.0
NE2 A:HIS181 4.8 14.0 1.0

Reference:

Y.Kim, N.Maltseva, M.Endres, A.Joachimiak, Center For Structural Genomics Of Infectious Diseases(Csgid). Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with the Hydrolyzed Penicillin G. To Be Published.
Page generated: Tue Oct 29 08:22:07 2024

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