Zinc in PDB 7zo2: L1 Metallo-Beta-Lactamase Complex with Hydrolysed Doripenem
Enzymatic activity of L1 Metallo-Beta-Lactamase Complex with Hydrolysed Doripenem
All present enzymatic activity of L1 Metallo-Beta-Lactamase Complex with Hydrolysed Doripenem:
3.5.2.6;
Protein crystallography data
The structure of L1 Metallo-Beta-Lactamase Complex with Hydrolysed Doripenem, PDB code: 7zo2
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 /
1.49
|
Space group
|
P 64 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
105.435,
105.435,
98.181,
90,
90,
120
|
R / Rfree (%)
|
17.6 /
20.5
|
Other elements in 7zo2:
The structure of L1 Metallo-Beta-Lactamase Complex with Hydrolysed Doripenem also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the L1 Metallo-Beta-Lactamase Complex with Hydrolysed Doripenem
(pdb code 7zo2). 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 Complex with Hydrolysed Doripenem, PDB code: 7zo2:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 7zo2
Go back to
Zinc Binding Sites List in 7zo2
Zinc binding site 1 out
of 2 in the L1 Metallo-Beta-Lactamase Complex with Hydrolysed Doripenem
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 Complex with Hydrolysed Doripenem within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn301
b:32.9
occ:1.00
|
OD2
|
A:ASP88
|
2.1
|
34.6
|
1.0
|
NAN
|
A:DQM305
|
2.1
|
95.7
|
1.0
|
NE2
|
A:HIS89
|
2.2
|
33.1
|
1.0
|
NE2
|
A:HIS225
|
2.2
|
32.8
|
1.0
|
OAX
|
A:DQM305
|
2.3
|
39.5
|
1.0
|
OAH
|
A:DQM305
|
2.4
|
31.6
|
1.0
|
CAS
|
A:DQM305
|
2.8
|
56.8
|
1.0
|
CG
|
A:ASP88
|
2.9
|
33.0
|
1.0
|
CAR
|
A:DQM305
|
3.0
|
54.5
|
1.0
|
CE1
|
A:HIS89
|
3.1
|
29.9
|
1.0
|
CD2
|
A:HIS225
|
3.1
|
36.0
|
1.0
|
CD2
|
A:HIS89
|
3.1
|
28.1
|
1.0
|
OD1
|
A:ASP88
|
3.2
|
27.7
|
1.0
|
CAJ
|
A:DQM305
|
3.2
|
62.2
|
1.0
|
HD2
|
A:HIS225
|
3.2
|
43.2
|
1.0
|
HE1
|
A:HIS89
|
3.2
|
35.9
|
1.0
|
CE1
|
A:HIS225
|
3.2
|
30.0
|
1.0
|
CAY
|
A:DQM305
|
3.3
|
98.7
|
1.0
|
HD2
|
A:HIS89
|
3.3
|
33.7
|
1.0
|
HE1
|
A:HIS225
|
3.5
|
36.0
|
1.0
|
H8
|
A:DQM305
|
3.6
|
118.6
|
1.0
|
CAX
|
A:DQM305
|
3.7
|
53.2
|
1.0
|
H3
|
A:DQM305
|
3.7
|
102.0
|
1.0
|
ZN
|
A:ZN302
|
3.8
|
29.6
|
1.0
|
HE1
|
A:HIS84
|
3.9
|
34.5
|
1.0
|
HG
|
A:SER185
|
4.0
|
37.9
|
1.0
|
ND1
|
A:HIS89
|
4.2
|
30.4
|
1.0
|
CAT
|
A:DQM305
|
4.2
|
84.8
|
1.0
|
CG
|
A:HIS89
|
4.2
|
29.0
|
1.0
|
OAE
|
A:DQM305
|
4.2
|
38.4
|
1.0
|
CB
|
A:ASP88
|
4.3
|
29.1
|
1.0
|
CAZ
|
A:DQM305
|
4.3
|
53.6
|
1.0
|
CG
|
A:HIS225
|
4.3
|
35.0
|
1.0
|
HB2
|
A:ASP88
|
4.3
|
35.0
|
1.0
|
ND1
|
A:HIS225
|
4.3
|
29.9
|
1.0
|
OAD
|
A:DQM305
|
4.3
|
43.6
|
1.0
|
NE2
|
A:HIS84
|
4.4
|
28.0
|
1.0
|
CE1
|
A:HIS84
|
4.5
|
28.8
|
1.0
|
CAU
|
A:DQM305
|
4.5
|
66.9
|
1.0
|
H2
|
A:DQM305
|
4.6
|
64.1
|
1.0
|
H17
|
A:DQM305
|
4.6
|
62.9
|
1.0
|
HH2
|
A:TRP17
|
4.7
|
39.0
|
1.0
|
H14
|
A:DQM305
|
4.7
|
64.5
|
1.0
|
H16
|
A:DQM305
|
4.7
|
62.9
|
1.0
|
OG
|
A:SER185
|
4.7
|
31.6
|
1.0
|
HZ3
|
A:TRP17
|
4.8
|
41.9
|
1.0
|
HB3
|
A:ASP88
|
4.8
|
35.0
|
1.0
|
HD21
|
A:LEU38
|
4.9
|
38.4
|
1.0
|
H9
|
A:DQM305
|
4.9
|
80.5
|
1.0
|
HB2
|
A:PRO224
|
4.9
|
37.1
|
1.0
|
HB2
|
A:HIS86
|
4.9
|
33.4
|
1.0
|
HD1
|
A:HIS89
|
4.9
|
36.5
|
1.0
|
|
Zinc binding site 2 out
of 2 in 7zo2
Go back to
Zinc Binding Sites List in 7zo2
Zinc binding site 2 out
of 2 in the L1 Metallo-Beta-Lactamase Complex with Hydrolysed Doripenem
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 Complex with Hydrolysed Doripenem within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn302
b:29.6
occ:1.00
|
OAX
|
A:DQM305
|
1.9
|
39.5
|
1.0
|
NE2
|
A:HIS160
|
2.1
|
28.0
|
1.0
|
NE2
|
A:HIS84
|
2.2
|
28.0
|
1.0
|
ND1
|
A:HIS86
|
2.2
|
28.0
|
1.0
|
CAJ
|
A:DQM305
|
2.5
|
62.2
|
1.0
|
OAD
|
A:DQM305
|
2.6
|
43.6
|
1.0
|
CD2
|
A:HIS160
|
3.0
|
27.8
|
1.0
|
HB2
|
A:HIS86
|
3.0
|
33.4
|
1.0
|
CD2
|
A:HIS84
|
3.0
|
29.2
|
1.0
|
HD2
|
A:HIS160
|
3.1
|
33.4
|
1.0
|
CE1
|
A:HIS84
|
3.1
|
28.8
|
1.0
|
CE1
|
A:HIS86
|
3.1
|
28.7
|
1.0
|
CG
|
A:HIS86
|
3.1
|
24.6
|
1.0
|
HD2
|
A:HIS84
|
3.2
|
35.0
|
1.0
|
CE1
|
A:HIS160
|
3.2
|
28.4
|
1.0
|
HE1
|
A:HIS86
|
3.3
|
34.4
|
1.0
|
HE1
|
A:HIS84
|
3.3
|
34.5
|
1.0
|
HE1
|
A:HIS160
|
3.4
|
34.0
|
1.0
|
CB
|
A:HIS86
|
3.5
|
27.9
|
1.0
|
OAH
|
A:DQM305
|
3.5
|
31.6
|
1.0
|
HD2
|
A:HIS89
|
3.5
|
33.7
|
1.0
|
HB3
|
A:HIS86
|
3.6
|
33.4
|
1.0
|
ZN
|
A:ZN301
|
3.8
|
32.9
|
1.0
|
H6
|
A:DQM305
|
4.0
|
95.4
|
1.0
|
CAX
|
A:DQM305
|
4.1
|
53.2
|
1.0
|
CG
|
A:HIS84
|
4.1
|
27.2
|
1.0
|
ND1
|
A:HIS84
|
4.1
|
29.6
|
1.0
|
CG
|
A:HIS160
|
4.1
|
28.9
|
1.0
|
CD2
|
A:HIS89
|
4.2
|
28.1
|
1.0
|
CAR
|
A:DQM305
|
4.2
|
54.5
|
1.0
|
ND1
|
A:HIS160
|
4.2
|
28.1
|
1.0
|
HE2
|
A:PHE124
|
4.2
|
50.4
|
1.0
|
NE2
|
A:HIS86
|
4.2
|
29.3
|
1.0
|
CD2
|
A:HIS86
|
4.3
|
26.2
|
1.0
|
OD1
|
A:ASP88
|
4.3
|
27.7
|
1.0
|
NE2
|
A:HIS89
|
4.4
|
33.1
|
1.0
|
HG23
|
A:THR161
|
4.4
|
34.9
|
1.0
|
HG
|
A:SER185
|
4.4
|
37.9
|
1.0
|
NAN
|
A:DQM305
|
4.5
|
95.7
|
1.0
|
H2
|
A:DQM305
|
4.5
|
64.1
|
1.0
|
CAS
|
A:DQM305
|
4.5
|
56.8
|
1.0
|
H3
|
A:DQM305
|
4.6
|
102.0
|
1.0
|
CAT
|
A:DQM305
|
4.7
|
84.8
|
1.0
|
CAA
|
A:DQM305
|
4.8
|
79.4
|
1.0
|
HB2
|
A:SER185
|
4.8
|
36.0
|
1.0
|
HZ
|
A:PHE124
|
4.8
|
46.3
|
1.0
|
HD1
|
A:HIS84
|
4.9
|
35.5
|
1.0
|
H
|
A:HIS86
|
4.9
|
29.9
|
1.0
|
CA
|
A:HIS86
|
4.9
|
25.2
|
1.0
|
CAY
|
A:DQM305
|
4.9
|
98.7
|
1.0
|
H14
|
A:DQM305
|
5.0
|
64.5
|
1.0
|
|
Reference:
P.Hinchliffe,
J.Spencer.
L1 Metallo-Beta-Lactamase Complex with Hydrolysed Doripenem To Be Published.
Page generated: Wed Oct 30 17:13:15 2024
|