Zinc in PDB 5wck: Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii
Enzymatic activity of Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii
All present enzymatic activity of Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii:
3.5.2.6;
Protein crystallography data
The structure of Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii, PDB code: 5wck
was solved by
I.Garcia-Saez,
P.S.Mercuri,
R.Kahn,
C.Papamicael,
I.G.Shabalin,
J.E.Raczynska,
M.Jaskolski,
W.Minor,
J.M.Frere,
M.Galleni,
O.Dideberg,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
24.93 /
1.65
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
44.860,
76.850,
78.890,
90.00,
102.08,
90.00
|
R / Rfree (%)
|
12.3 /
15.8
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii
(pdb code 5wck). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii, PDB code: 5wck:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 5wck
Go back to
Zinc Binding Sites List in 5wck
Zinc binding site 1 out
of 4 in the Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn301
b:11.2
occ:1.00
|
O
|
A:HOH580
|
2.0
|
18.7
|
1.0
|
OD2
|
A:ASP94
|
2.0
|
9.5
|
1.0
|
NE2
|
A:HIS234
|
2.1
|
7.2
|
1.0
|
NE2
|
A:HIS95
|
2.1
|
6.2
|
1.0
|
UNK
|
A:UNX313
|
2.2
|
16.4
|
1.0
|
UNK
|
A:UNX312
|
2.3
|
17.6
|
1.0
|
CG
|
A:ASP94
|
3.0
|
8.4
|
1.0
|
CE1
|
A:HIS234
|
3.0
|
9.9
|
1.0
|
CE1
|
A:HIS95
|
3.0
|
6.1
|
1.0
|
CD2
|
A:HIS234
|
3.1
|
9.0
|
1.0
|
CD2
|
A:HIS95
|
3.1
|
6.1
|
1.0
|
OD1
|
A:ASP94
|
3.3
|
9.3
|
1.0
|
UNK
|
A:UNX309
|
3.4
|
11.5
|
1.0
|
ZN
|
A:ZN302
|
3.7
|
8.5
|
1.0
|
NE2
|
A:HIS90
|
4.1
|
6.9
|
1.0
|
CE1
|
A:HIS90
|
4.1
|
7.9
|
1.0
|
ND1
|
A:HIS234
|
4.1
|
8.1
|
1.0
|
UNK
|
A:UNX310
|
4.1
|
16.5
|
1.0
|
ND1
|
A:HIS95
|
4.2
|
6.9
|
1.0
|
UNK
|
A:UNX314
|
4.2
|
16.4
|
1.0
|
CG
|
A:HIS234
|
4.2
|
7.7
|
1.0
|
CG
|
A:HIS95
|
4.2
|
5.0
|
1.0
|
CB
|
A:ASP94
|
4.3
|
9.7
|
1.0
|
O
|
A:HOH552
|
4.7
|
32.3
|
1.0
|
UNK
|
A:UNX311
|
4.8
|
41.6
|
1.0
|
OG
|
A:SER233
|
5.0
|
6.8
|
1.0
|
NE2
|
A:HIS168
|
5.0
|
5.8
|
1.0
|
|
Zinc binding site 2 out
of 4 in 5wck
Go back to
Zinc Binding Sites List in 5wck
Zinc binding site 2 out
of 4 in the Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn302
b:8.5
occ:1.00
|
O
|
A:HOH580
|
2.0
|
18.7
|
1.0
|
ND1
|
A:HIS92
|
2.1
|
8.1
|
1.0
|
NE2
|
A:HIS168
|
2.1
|
5.8
|
1.0
|
NE2
|
A:HIS90
|
2.1
|
6.9
|
1.0
|
UNK
|
A:UNX310
|
2.4
|
16.5
|
1.0
|
CE1
|
A:HIS92
|
3.0
|
6.5
|
1.0
|
CE1
|
A:HIS90
|
3.0
|
7.9
|
1.0
|
CD2
|
A:HIS168
|
3.0
|
5.3
|
1.0
|
CD2
|
A:HIS90
|
3.1
|
6.5
|
1.0
|
CE1
|
A:HIS168
|
3.1
|
6.3
|
1.0
|
CG
|
A:HIS92
|
3.1
|
7.2
|
1.0
|
UNK
|
A:UNX313
|
3.3
|
16.4
|
1.0
|
CB
|
A:HIS92
|
3.5
|
6.3
|
1.0
|
UNK
|
A:UNX309
|
3.6
|
11.5
|
1.0
|
ZN
|
A:ZN301
|
3.7
|
11.2
|
1.0
|
ND1
|
A:HIS90
|
4.1
|
5.3
|
1.0
|
NE2
|
A:HIS92
|
4.1
|
8.4
|
1.0
|
CG
|
A:HIS90
|
4.2
|
6.1
|
1.0
|
UNK
|
A:UNX312
|
4.2
|
17.6
|
1.0
|
OD1
|
A:ASP94
|
4.2
|
9.3
|
1.0
|
CG
|
A:HIS168
|
4.2
|
6.1
|
1.0
|
ND1
|
A:HIS168
|
4.2
|
6.2
|
1.0
|
CD2
|
A:HIS92
|
4.2
|
8.8
|
1.0
|
CD2
|
A:HIS95
|
4.3
|
6.1
|
1.0
|
NE2
|
A:HIS95
|
4.4
|
6.2
|
1.0
|
UNK
|
A:UNX311
|
4.4
|
41.6
|
1.0
|
UNK
|
A:UNX314
|
4.5
|
16.4
|
1.0
|
ND2
|
A:ASN197
|
4.6
|
11.2
|
1.0
|
OD2
|
A:ASP94
|
4.8
|
9.5
|
1.0
|
CG
|
A:ASP94
|
4.9
|
8.4
|
1.0
|
CG2
|
A:THR169
|
5.0
|
7.5
|
1.0
|
CA
|
A:HIS92
|
5.0
|
7.1
|
1.0
|
|
Zinc binding site 3 out
of 4 in 5wck
Go back to
Zinc Binding Sites List in 5wck
Zinc binding site 3 out
of 4 in the Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn301
b:11.5
occ:1.00
|
O
|
B:HOH549
|
2.0
|
20.8
|
1.0
|
OD2
|
B:ASP94
|
2.0
|
10.6
|
1.0
|
NE2
|
B:HIS234
|
2.1
|
7.5
|
1.0
|
NE2
|
B:HIS95
|
2.1
|
6.3
|
1.0
|
UNK
|
B:UNX310
|
2.3
|
15.2
|
1.0
|
UNK
|
B:UNX309
|
2.3
|
15.2
|
1.0
|
CG
|
B:ASP94
|
3.0
|
9.3
|
1.0
|
CE1
|
B:HIS234
|
3.0
|
9.9
|
1.0
|
CE1
|
B:HIS95
|
3.1
|
7.3
|
1.0
|
CD2
|
B:HIS234
|
3.1
|
8.7
|
1.0
|
CD2
|
B:HIS95
|
3.1
|
7.5
|
1.0
|
OD1
|
B:ASP94
|
3.2
|
10.4
|
1.0
|
UNK
|
B:UNX312
|
3.4
|
14.1
|
1.0
|
ZN
|
B:ZN302
|
3.7
|
8.9
|
1.0
|
NE2
|
B:HIS90
|
4.0
|
6.9
|
1.0
|
UNK
|
B:UNX314
|
4.0
|
40.9
|
1.0
|
CE1
|
B:HIS90
|
4.1
|
7.0
|
1.0
|
ND1
|
B:HIS234
|
4.2
|
7.9
|
1.0
|
ND1
|
B:HIS95
|
4.2
|
7.7
|
1.0
|
CG
|
B:HIS95
|
4.2
|
5.5
|
1.0
|
CG
|
B:HIS234
|
4.2
|
7.6
|
1.0
|
UNK
|
B:UNX311
|
4.2
|
17.7
|
1.0
|
UNK
|
B:UNX313
|
4.2
|
14.8
|
1.0
|
CB
|
B:ASP94
|
4.3
|
9.2
|
1.0
|
O
|
B:HOH648
|
4.6
|
33.0
|
1.0
|
NE2
|
B:HIS168
|
5.0
|
6.8
|
1.0
|
OG
|
B:SER233
|
5.0
|
8.5
|
1.0
|
|
Zinc binding site 4 out
of 4 in 5wck
Go back to
Zinc Binding Sites List in 5wck
Zinc binding site 4 out
of 4 in the Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn302
b:8.9
occ:1.00
|
O
|
B:HOH549
|
2.0
|
20.8
|
1.0
|
ND1
|
B:HIS92
|
2.1
|
7.2
|
1.0
|
NE2
|
B:HIS168
|
2.1
|
6.8
|
1.0
|
NE2
|
B:HIS90
|
2.1
|
6.9
|
1.0
|
UNK
|
B:UNX313
|
2.4
|
14.8
|
1.0
|
CE1
|
B:HIS92
|
3.0
|
6.9
|
1.0
|
CD2
|
B:HIS168
|
3.0
|
5.6
|
1.0
|
CD2
|
B:HIS90
|
3.0
|
5.5
|
1.0
|
CE1
|
B:HIS90
|
3.0
|
7.0
|
1.0
|
CE1
|
B:HIS168
|
3.1
|
7.7
|
1.0
|
CG
|
B:HIS92
|
3.1
|
6.3
|
1.0
|
UNK
|
B:UNX310
|
3.3
|
15.2
|
1.0
|
UNK
|
B:UNX312
|
3.5
|
14.1
|
1.0
|
CB
|
B:HIS92
|
3.5
|
6.0
|
1.0
|
ZN
|
B:ZN301
|
3.7
|
11.5
|
1.0
|
ND1
|
B:HIS90
|
4.1
|
7.1
|
1.0
|
NE2
|
B:HIS92
|
4.1
|
9.6
|
1.0
|
CG
|
B:HIS90
|
4.1
|
6.5
|
1.0
|
UNK
|
B:UNX309
|
4.2
|
15.2
|
1.0
|
OD1
|
B:ASP94
|
4.2
|
10.4
|
1.0
|
CG
|
B:HIS168
|
4.2
|
5.8
|
1.0
|
CD2
|
B:HIS92
|
4.2
|
8.8
|
1.0
|
ND1
|
B:HIS168
|
4.2
|
7.7
|
1.0
|
CD2
|
B:HIS95
|
4.3
|
7.5
|
1.0
|
O
|
B:HOH726
|
4.3
|
36.9
|
1.0
|
NE2
|
B:HIS95
|
4.4
|
6.3
|
1.0
|
UNK
|
B:UNX311
|
4.6
|
17.7
|
1.0
|
ND2
|
B:ASN197
|
4.6
|
12.5
|
1.0
|
UNK
|
B:UNX314
|
4.7
|
40.9
|
1.0
|
OD2
|
B:ASP94
|
4.8
|
10.6
|
1.0
|
CG
|
B:ASP94
|
4.9
|
9.3
|
1.0
|
CG2
|
B:THR169
|
4.9
|
7.8
|
1.0
|
CA
|
B:HIS92
|
5.0
|
6.6
|
1.0
|
|
Reference:
I.Garcia-Saez,
P.S.Mercuri,
C.Papamicael,
R.Kahn,
J.M.Frere,
M.Galleni,
G.M.Rossolini,
O.Dideberg.
Three-Dimensional Structure of Fez-1, A Monomeric Subclass B3 Metallo-Beta-Lactamase From Fluoribacter Gormanii, in Native Form and in Complex with D-Captopril. J. Mol. Biol. V. 325 651 2003.
ISSN: ISSN 0022-2836
PubMed: 12507470
Page generated: Mon Oct 28 14:05:30 2024
|