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Zinc in PDB 2aio: Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Complexed with Hydrolyzed Moxalactam

Enzymatic activity of Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Complexed with Hydrolyzed Moxalactam

All present enzymatic activity of Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Complexed with Hydrolyzed Moxalactam:
3.5.2.6;

Protein crystallography data

The structure of Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Complexed with Hydrolyzed Moxalactam, PDB code: 2aio was solved by J.Spencer, J.Read, R.B.Sessions, S.Howell, G.M.Blackburn, S.J.Gamblin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.99 / 1.70
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 105.024, 105.024, 98.230, 90.00, 90.00, 120.00
R / Rfree (%) 17.1 / 20

Zinc Binding Sites:

The binding sites of Zinc atom in the Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Complexed with Hydrolyzed Moxalactam (pdb code 2aio). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Complexed with Hydrolyzed Moxalactam, PDB code: 2aio:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2aio

Go back to Zinc Binding Sites List in 2aio
Zinc binding site 1 out of 2 in the Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Complexed with Hydrolyzed Moxalactam


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Complexed with Hydrolyzed Moxalactam within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn314

b:15.9
occ:1.00
NE2 A:HIS121 2.1 13.5 1.0
NE2 A:HIS263 2.1 11.3 1.0
O A:HOH600 2.2 15.5 1.0
OD2 A:ASP120 2.2 13.8 1.0
O3 A:MX11 2.3 14.6 1.0
N1 A:MX11 2.4 15.5 1.0
CE1 A:HIS121 3.0 14.2 1.0
C7 A:MX11 3.0 14.4 1.0
CG A:ASP120 3.0 12.7 1.0
CE1 A:HIS263 3.1 12.2 1.0
C4 A:MX11 3.1 15.5 1.0
CD2 A:HIS121 3.1 13.5 1.0
CD2 A:HIS263 3.1 10.4 1.0
OD1 A:ASP120 3.3 11.9 1.0
C3 A:MX11 3.4 14.7 1.0
ZN A:ZN315 3.7 14.8 1.0
O5 A:MX11 4.0 13.8 1.0
ND1 A:HIS121 4.1 13.9 1.0
CG A:HIS121 4.2 14.4 1.0
ND1 A:HIS263 4.2 12.4 1.0
NE2 A:HIS116 4.2 12.7 1.0
C2 A:MX11 4.2 15.0 1.0
O32 A:MX11 4.2 14.7 1.0
CE1 A:HIS116 4.2 12.8 1.0
O4 A:MX11 4.2 13.3 1.0
CG A:HIS263 4.2 13.1 1.0
CB A:ASP120 4.4 13.0 1.0
C5 A:MX11 4.4 16.3 1.0
OG A:SER221 4.5 13.8 1.0
O2 A:MX11 4.5 15.3 1.0
C1 A:MX11 4.5 16.1 1.0
NE2 A:HIS196 4.8 13.0 1.0

Zinc binding site 2 out of 2 in 2aio

Go back to Zinc Binding Sites List in 2aio
Zinc binding site 2 out of 2 in the Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Complexed with Hydrolyzed Moxalactam


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Complexed with Hydrolyzed Moxalactam within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn315

b:14.8
occ:1.00
O A:HOH600 2.0 15.5 1.0
NE2 A:HIS196 2.1 13.0 1.0
ND1 A:HIS118 2.1 12.2 1.0
NE2 A:HIS116 2.2 12.7 1.0
O32 A:MX11 2.4 14.7 1.0
CD2 A:HIS196 3.0 12.3 1.0
CE1 A:HIS118 3.0 11.4 1.0
CG A:HIS118 3.1 11.7 1.0
CD2 A:HIS116 3.1 11.2 1.0
CE1 A:HIS196 3.1 13.0 1.0
CE1 A:HIS116 3.1 12.8 1.0
CB A:HIS118 3.4 11.7 1.0
O3 A:MX11 3.5 14.6 1.0
C1 A:MX11 3.6 16.1 1.0
ZN A:ZN314 3.7 15.9 1.0
N1 A:MX11 4.0 15.5 1.0
O5 A:MX11 4.0 13.8 1.0
NE2 A:HIS118 4.1 10.6 1.0
CG A:HIS196 4.1 12.1 1.0
OD1 A:ASP120 4.2 11.9 1.0
C7 A:MX11 4.2 14.4 1.0
CD2 A:HIS118 4.2 11.7 1.0
ND1 A:HIS196 4.2 12.3 1.0
ND1 A:HIS116 4.2 13.4 1.0
CG A:HIS116 4.2 12.2 1.0
CD2 A:HIS121 4.3 13.5 1.0
C9 A:MX11 4.3 13.2 1.0
C2 A:MX11 4.4 15.0 1.0
NE2 A:HIS121 4.4 13.5 1.0
C4 A:MX11 4.4 15.5 1.0
O31 A:MX11 4.5 16.8 1.0
C3 A:MX11 4.8 14.7 1.0
OD2 A:ASP120 4.9 13.8 1.0
CA A:HIS118 4.9 12.0 1.0
CG A:ASP120 5.0 12.7 1.0

Reference:

J.Spencer, J.Read, R.B.Sessions, S.Howell, G.M.Blackburn, S.J.Gamblin. Antibiotic Recognition By Binuclear Metallo-Beta-Lactamases Revealed By X-Ray Crystallography J.Am.Chem.Soc. V. 127 14439 2005.
ISSN: ISSN 0002-7863
PubMed: 16218639
DOI: 10.1021/JA0536062
Page generated: Wed Dec 16 03:17:37 2020

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