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Zinc in PDB 2fu9: Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (MP2 Inhibitor Complex)

Enzymatic activity of Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (MP2 Inhibitor Complex)

All present enzymatic activity of Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (MP2 Inhibitor Complex):
3.5.2.6;

Protein crystallography data

The structure of Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (MP2 Inhibitor Complex), PDB code: 2fu9 was solved by L.Nauton, G.Garau, R.Kahn, O.Dideberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.46 / 1.80
Space group P 62 2 2
Cell size a, b, c (Å), α, β, γ (°) 105.050, 105.050, 196.700, 90.00, 90.00, 120.00
R / Rfree (%) 14.9 / 18.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (MP2 Inhibitor Complex) (pdb code 2fu9). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (MP2 Inhibitor Complex), PDB code: 2fu9:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 2fu9

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Zinc binding site 1 out of 4 in the Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (MP2 Inhibitor Complex)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (MP2 Inhibitor Complex) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:14.0
occ:1.00
NE2 A:HIS196 2.0 11.8 1.0
NE2 A:HIS116 2.1 9.5 1.0
ND1 A:HIS118 2.1 12.2 1.0
S21 A:MP21410 2.3 15.7 1.0
CD2 A:HIS196 2.9 11.0 1.0
CD2 A:HIS116 3.0 10.3 1.0
CE1 A:HIS118 3.0 11.0 1.0
CE1 A:HIS116 3.1 10.3 1.0
O A:HOH1641 3.1 26.4 1.0
CE1 A:HIS196 3.1 11.4 1.0
CG A:HIS118 3.2 11.9 1.0
C17 A:MP21410 3.3 24.5 1.0
CB A:HIS118 3.5 11.7 1.0
ZN A:ZN402 3.7 14.2 1.0
CG A:HIS196 4.1 11.8 1.0
CG A:HIS116 4.1 9.5 1.0
ND1 A:HIS116 4.1 9.7 1.0
ND1 A:HIS196 4.2 10.9 1.0
NE2 A:HIS118 4.2 10.2 1.0
CD2 A:HIS121 4.3 10.1 1.0
CD2 A:HIS118 4.3 11.0 1.0
OD1 A:ASP120 4.3 11.7 1.0
NE2 A:HIS121 4.3 11.1 1.0
C15 A:MP21410 4.4 29.8 1.0
O A:HOH1630 4.9 25.6 1.0
CA A:HIS118 5.0 11.2 1.0
OH A:TYR229 5.0 11.2 1.0

Zinc binding site 2 out of 4 in 2fu9

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Zinc binding site 2 out of 4 in the Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (MP2 Inhibitor Complex)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (MP2 Inhibitor Complex) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn402

b:14.2
occ:1.00
OD2 A:ASP120 2.0 12.9 1.0
NE2 A:HIS263 2.0 10.8 1.0
NE2 A:HIS121 2.1 11.1 1.0
S21 A:MP21410 2.3 15.7 1.0
O A:HOH1641 2.7 26.4 1.0
CG A:ASP120 2.8 11.1 1.0
OD1 A:ASP120 2.9 11.7 1.0
CE1 A:HIS263 3.0 11.3 1.0
CE1 A:HIS121 3.0 9.9 1.0
CD2 A:HIS263 3.1 12.1 1.0
CD2 A:HIS121 3.1 10.1 1.0
C17 A:MP21410 3.3 24.5 1.0
ZN A:ZN401 3.7 14.0 1.0
ND1 A:HIS121 4.1 10.7 1.0
ND1 A:HIS263 4.1 10.2 1.0
CG A:HIS121 4.2 10.3 1.0
CG A:HIS263 4.2 12.4 1.0
CB A:ASP120 4.2 10.9 1.0
NE2 A:HIS116 4.3 9.5 1.0
C13 A:MP21410 4.3 34.0 1.0
N A:MP21410 4.3 35.0 1.0
C15 A:MP21410 4.3 29.8 1.0
CE1 A:HIS116 4.3 10.3 1.0
O A:HOH1630 4.5 25.6 1.0
CA A:MP21410 4.5 36.7 1.0
C A:MP21410 4.6 37.4 1.0
O1 A:MP21410 4.7 38.4 1.0
O14 A:MP21410 4.7 34.0 1.0
OG A:SER221 4.9 19.1 1.0

Zinc binding site 3 out of 4 in 2fu9

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Zinc binding site 3 out of 4 in the Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (MP2 Inhibitor Complex)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (MP2 Inhibitor Complex) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn401

b:15.6
occ:1.00
NE2 B:HIS116 2.0 12.3 1.0
NE2 B:HIS196 2.1 12.6 1.0
ND1 B:HIS118 2.1 11.6 1.0
S21 B:MP22410 2.2 16.2 1.0
CD2 B:HIS196 2.9 14.0 1.0
CD2 B:HIS116 2.9 12.2 1.0
CE1 B:HIS116 3.0 11.4 1.0
CE1 B:HIS118 3.0 13.1 1.0
O B:HOH2580 3.1 31.6 1.0
CG B:HIS118 3.1 12.1 1.0
CE1 B:HIS196 3.2 13.1 1.0
C17 B:MP22410 3.3 23.0 1.0
CB B:HIS118 3.5 11.3 1.0
ZN B:ZN402 3.7 16.1 1.0
ND1 B:HIS116 4.0 13.2 1.0
CG B:HIS116 4.0 12.8 1.0
CG B:HIS196 4.1 12.1 1.0
NE2 B:HIS118 4.2 12.1 1.0
ND1 B:HIS196 4.2 13.0 1.0
CD2 B:HIS121 4.2 12.4 1.0
CD2 B:HIS118 4.2 11.1 1.0
OD1 B:ASP120 4.3 12.2 1.0
NE2 B:HIS121 4.3 12.7 1.0
C15 B:MP22410 4.3 28.7 1.0
CA B:HIS118 4.9 11.5 1.0
CG2 B:THR197 5.0 11.8 1.0

Zinc binding site 4 out of 4 in 2fu9

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Zinc binding site 4 out of 4 in the Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (MP2 Inhibitor Complex)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (MP2 Inhibitor Complex) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn402

b:16.1
occ:1.00
OD2 B:ASP120 2.0 13.3 1.0
NE2 B:HIS121 2.0 12.7 1.0
NE2 B:HIS263 2.1 9.0 1.0
S21 B:MP22410 2.3 16.2 1.0
CG B:ASP120 2.8 13.2 1.0
O B:HOH2580 2.9 31.6 1.0
CE1 B:HIS263 2.9 11.6 1.0
CE1 B:HIS121 2.9 11.5 1.0
OD1 B:ASP120 3.0 12.2 1.0
CD2 B:HIS121 3.1 12.4 1.0
CD2 B:HIS263 3.1 12.2 1.0
C17 B:MP22410 3.3 23.0 1.0
ZN B:ZN401 3.7 15.6 1.0
ND1 B:HIS121 4.0 12.1 1.0
ND1 B:HIS263 4.1 11.4 1.0
CG B:HIS121 4.1 12.7 1.0
CB B:ASP120 4.2 12.4 1.0
CG B:HIS263 4.2 13.0 1.0
NE2 B:HIS116 4.2 12.3 1.0
N B:MP22410 4.3 34.7 1.0
CE1 B:HIS116 4.3 11.4 1.0
C13 B:MP22410 4.3 33.3 1.0
C15 B:MP22410 4.4 28.7 1.0
O B:HOH2508 4.5 30.5 1.0
CA B:MP22410 4.7 36.0 1.0
O14 B:MP22410 4.8 35.3 1.0
CH2 B:TRP39 4.9 17.6 1.0
C B:MP22410 4.9 37.0 1.0
CZ3 B:TRP39 5.0 16.3 1.0
OG B:SER221 5.0 18.1 1.0

Reference:

L.Nauton, R.Kahn, G.Garau, J.F.Hernandez, O.Dideberg. Structural Insights Into the Design of Inhibitors For the L1 Metallo-Beta-Lactamase From Stenotrophomonas Maltophilia. J.Mol.Biol. V. 375 257 2008.
ISSN: ISSN 0022-2836
PubMed: 17999929
DOI: 10.1016/J.JMB.2007.10.036
Page generated: Wed Dec 16 03:28:38 2020

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