Zinc in PDB 7zo7: L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Cefmetazole

Enzymatic activity of L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Cefmetazole

All present enzymatic activity of L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Cefmetazole:
3.5.2.6;

Protein crystallography data

The structure of L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Cefmetazole, PDB code: 7zo7 was solved by P.Hinchliffe, J.Spencer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 66.86 / 1.63
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 105.469, 105.469, 98.135, 90, 90, 120
R / Rfree (%) 15.9 / 17.5

Zinc Binding Sites:

The binding sites of Zinc atom in the L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Cefmetazole (pdb code 7zo7). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Cefmetazole, PDB code: 7zo7:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 7zo7

Go back to Zinc Binding Sites List in 7zo7
Zinc binding site 1 out of 2 in the L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Cefmetazole


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Cefmetazole within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:21.8
occ:1.00
O A:HOH411 1.9 26.2 1.0
NE2 A:HIS160 2.0 19.0 1.0
NE2 A:HIS84 2.1 19.9 1.0
ND1 A:HIS86 2.1 22.0 1.0
O19 A:JOU304 2.5 31.9 1.0
CD2 A:HIS160 2.9 18.7 1.0
HD2 A:HIS160 3.0 22.5 1.0
CD2 A:HIS84 3.0 20.2 1.0
CE1 A:HIS86 3.0 21.4 1.0
CE1 A:HIS84 3.0 21.3 1.0
HB2 A:HIS86 3.0 23.8 1.0
CG A:HIS86 3.1 19.7 1.0
CE1 A:HIS160 3.1 23.1 1.0
HE1 A:HIS86 3.2 25.7 1.0
HD2 A:HIS84 3.2 24.2 1.0
HE1 A:HIS84 3.2 25.5 1.0
H173 A:JOU304 3.3 46.8 1.0
HE1 A:HIS160 3.4 27.8 1.0
O03 A:JOU304 3.4 24.9 1.0
CB A:HIS86 3.5 19.8 1.0
HD2 A:HIS89 3.5 28.1 1.0
HB3 A:HIS86 3.6 23.8 1.0
ZN A:ZN302 3.7 25.8 1.0
C18 A:JOU304 3.7 51.4 1.0
ND1 A:HIS84 4.1 20.2 1.0
CG A:HIS160 4.1 20.6 1.0
N05 A:JOU304 4.1 32.7 1.0
CG A:HIS84 4.1 19.1 1.0
NE2 A:HIS86 4.1 21.2 1.0
OD1 A:ASP88 4.2 23.0 1.0
ND1 A:HIS160 4.2 20.5 1.0
C02 A:JOU304 4.2 30.6 1.0
C17 A:JOU304 4.2 39.0 1.0
CD2 A:HIS86 4.2 19.4 1.0
O16 A:JOU304 4.2 41.6 1.0
CD2 A:HIS89 4.2 23.4 1.0
HG23 A:THR161 4.4 24.0 1.0
NE2 A:HIS89 4.4 26.1 1.0
HE2 A:PHE124 4.4 54.4 1.0
HG A:SER185 4.4 21.7 0.6
C04 A:JOU304 4.4 33.6 1.0
C07 A:JOU304 4.5 52.7 1.0
O20 A:JOU304 4.7 55.5 1.0
H172 A:JOU304 4.8 46.8 1.0
HB3 A:SER185 4.8 26.2 0.4
HB2 A:SER185 4.9 25.9 0.6
HD1 A:HIS84 4.9 24.3 1.0
H171 A:JOU304 4.9 46.8 1.0
H A:HIS86 4.9 22.1 1.0
HE2 A:HIS86 4.9 25.4 1.0
CA A:HIS86 4.9 19.3 1.0
OD2 A:ASP88 4.9 25.8 1.0
HD1 A:HIS160 5.0 24.6 1.0
HG21 A:THR161 5.0 24.0 1.0
CG A:ASP88 5.0 26.7 1.0

Zinc binding site 2 out of 2 in 7zo7

Go back to Zinc Binding Sites List in 7zo7
Zinc binding site 2 out of 2 in the L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Cefmetazole


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Cefmetazole within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:25.8
occ:1.00
NE2 A:HIS225 2.1 24.5 1.0
NE2 A:HIS89 2.1 26.1 1.0
OD2 A:ASP88 2.2 25.8 1.0
O A:HOH411 2.2 26.2 1.0
O03 A:JOU304 2.2 24.9 1.0
N05 A:JOU304 2.4 32.7 1.0
CD2 A:HIS225 3.0 23.8 1.0
CG A:ASP88 3.0 26.7 1.0
CE1 A:HIS89 3.0 26.9 1.0
CD2 A:HIS89 3.1 23.4 1.0
C02 A:JOU304 3.1 30.6 1.0
CE1 A:HIS225 3.1 25.6 1.0
HD2 A:HIS225 3.1 28.6 1.0
HE1 A:HIS89 3.2 32.2 1.0
C04 A:JOU304 3.2 33.6 1.0
OD1 A:ASP88 3.3 23.0 1.0
HD2 A:HIS89 3.3 28.1 1.0
HE1 A:HIS225 3.3 30.7 1.0
H061 A:JOU304 3.4 71.3 1.0
C06 A:JOU304 3.5 59.4 1.0
HE1 A:HIS84 3.6 25.5 1.0
ZN A:ZN301 3.7 21.8 1.0
HG A:SER185 3.8 21.7 0.6
O16 A:JOU304 3.9 41.6 1.0
O19 A:JOU304 4.1 31.9 1.0
ND1 A:HIS89 4.1 22.9 1.0
CG A:HIS225 4.2 25.6 1.0
ND1 A:HIS225 4.2 25.3 1.0
CG A:HIS89 4.2 21.2 1.0
C07 A:JOU304 4.2 52.7 1.0
O01 A:JOU304 4.2 28.6 1.0
CE1 A:HIS84 4.2 21.3 1.0
NE2 A:HIS84 4.3 19.9 1.0
H242 A:JOU304 4.3 75.9 1.0
CB A:ASP88 4.4 20.0 1.0
HB2 A:ASP88 4.4 24.0 1.0
C18 A:JOU304 4.4 51.4 1.0
H241 A:JOU304 4.5 75.9 1.0
OG A:SER185 4.5 18.1 0.6
C23 A:JOU304 4.6 41.6 1.0
C24 A:JOU304 4.7 63.3 1.0
HH2 A:TRP17 4.8 33.7 1.0
NE2 A:HIS160 4.8 19.0 1.0
H173 A:JOU304 4.8 46.8 1.0
HB2 A:PRO224 4.8 25.6 1.0
S21 A:JOU304 4.9 35.8 1.0
HB2 A:HIS86 4.9 23.8 1.0
HB2 A:SER185 4.9 26.2 0.4
HB3 A:ASP88 4.9 24.0 1.0
HD1 A:HIS89 4.9 27.4 1.0
HZ3 A:TRP17 4.9 30.2 1.0
C17 A:JOU304 4.9 39.0 1.0
HD1 A:HIS225 5.0 30.4 1.0

Reference:

P.Hinchliffe, J.Spencer. L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Cefmetazole To Be Published.
Page generated: Sat Apr 8 07:13:31 2023

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