Zinc in PDB 6u0y: Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia

Enzymatic activity of Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia

All present enzymatic activity of Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia, PDB code: 6u0y was solved by Y.Kim, N.Maltseva, M.Endres, A.Joachimiak, Center For Structural Genomicsof Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.63 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 68.033, 97.229, 91.725, 90.00, 105.55, 90.00
R / Rfree (%) 16.8 / 19.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (pdb code 6u0y). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia, PDB code: 6u0y:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Zinc binding site 1 out of 8 in 6u0y

Go back to Zinc Binding Sites List in 6u0y
Zinc binding site 1 out of 8 in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia


Mono view


Stereo pair view

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

b:27.9
occ:0.86
NE2 A:HIS181 2.1 23.3 1.0
ND1 A:HIS107 2.2 22.1 1.0
O1 A:EDO305 2.2 31.9 1.0
NE2 A:HIS105 2.2 30.6 1.0
O2 A:EDO305 2.4 29.2 1.0
CE1 A:HIS107 3.1 24.9 1.0
CE1 A:HIS181 3.1 26.7 1.0
CE1 A:HIS105 3.1 26.7 1.0
CD2 A:HIS181 3.1 19.6 1.0
C2 A:EDO305 3.2 30.9 1.0
CG A:HIS107 3.2 21.9 1.0
CD2 A:HIS105 3.2 22.4 1.0
C1 A:EDO305 3.2 32.4 1.0
ZN A:ZN302 3.5 41.4 0.6
CB A:HIS107 3.6 23.3 1.0
NE2 A:HIS107 4.2 22.0 1.0
ND1 A:HIS181 4.2 22.5 1.0
ND1 A:HIS105 4.2 27.2 1.0
OD1 A:ASP109 4.3 28.1 1.0
CG A:HIS181 4.3 20.5 1.0
CG A:HIS105 4.3 25.2 1.0
CD2 A:HIS107 4.3 22.5 1.0
CD2 A:HIS110 4.4 26.0 1.0
NE2 A:HIS110 4.6 29.2 1.0

Zinc binding site 2 out of 8 in 6u0y

Go back to Zinc Binding Sites List in 6u0y
Zinc binding site 2 out of 8 in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia


Mono view


Stereo pair view

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

b:41.4
occ:0.57
NE2 A:HIS110 2.1 29.2 1.0
NE2 A:HIS246 2.5 38.6 1.0
O1 A:EDO305 2.9 31.9 1.0
CD2 A:HIS110 2.9 26.0 1.0
OD2 A:ASP109 3.0 38.4 1.0
CE1 A:HIS110 3.3 30.4 1.0
OD1 A:ASP109 3.3 28.1 1.0
CG A:ASP109 3.4 36.1 1.0
CD2 A:HIS246 3.4 37.2 1.0
ZN A:ZN301 3.5 27.9 0.9
CE1 A:HIS246 3.5 34.3 1.0
C1 A:EDO305 3.9 32.4 1.0
CE1 A:HIS105 4.0 26.7 1.0
NE2 A:HIS105 4.1 30.6 1.0
CG A:HIS110 4.2 27.6 1.0
ND1 A:HIS110 4.3 24.7 1.0
O2 A:EDO305 4.3 29.2 1.0
ND1 A:HIS246 4.6 36.2 1.0
CG A:HIS246 4.6 31.4 1.0
CB A:ASP109 4.6 24.0 1.0
OG A:SER206 4.6 22.4 0.3
NE2 A:HIS181 4.7 23.3 1.0
C2 A:EDO305 4.8 30.9 1.0

Zinc binding site 3 out of 8 in 6u0y

Go back to Zinc Binding Sites List in 6u0y
Zinc binding site 3 out of 8 in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn300

b:30.3
occ:0.78
O B:HOH402 2.1 37.9 1.0
NE2 B:HIS181 2.1 25.0 1.0
ND1 B:HIS107 2.2 30.4 1.0
NE2 B:HIS105 2.2 30.9 1.0
O2 B:EDO302 2.5 48.7 1.0
O B:HOH468 2.8 34.2 1.0
CD2 B:HIS181 3.1 25.3 1.0
CE1 B:HIS181 3.1 29.0 1.0
CE1 B:HIS107 3.1 28.2 1.0
CE1 B:HIS105 3.1 27.8 1.0
CD2 B:HIS105 3.2 24.8 1.0
CG B:HIS107 3.2 22.0 1.0
ZN B:ZN301 3.4 34.6 0.7
CB B:HIS107 3.5 20.6 1.0
C2 B:EDO302 3.7 60.2 1.0
O1 B:EDO302 3.8 59.7 1.0
ND1 B:HIS105 4.2 31.3 1.0
ND1 B:HIS181 4.2 25.3 1.0
CG B:HIS181 4.2 24.2 1.0
NE2 B:HIS107 4.2 27.6 1.0
CG B:HIS105 4.3 22.9 1.0
OD1 B:ASP109 4.3 30.9 1.0
CD2 B:HIS110 4.3 25.4 1.0
CD2 B:HIS107 4.3 24.4 1.0
C1 B:EDO302 4.3 65.4 1.0
NE2 B:HIS110 4.5 28.7 1.0
OD2 B:ASP109 4.8 37.7 1.0
O B:HOH485 5.0 37.2 1.0
CG B:ASP109 5.0 34.6 1.0

Zinc binding site 4 out of 8 in 6u0y

Go back to Zinc Binding Sites List in 6u0y
Zinc binding site 4 out of 8 in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn301

b:34.6
occ:0.74
O B:HOH468 2.2 34.2 1.0
NE2 B:HIS246 2.2 30.8 1.0
NE2 B:HIS110 2.2 28.7 1.0
OD2 B:ASP109 2.3 37.7 1.0
O B:HOH402 2.3 37.9 1.0
O1 B:EDO302 2.4 59.7 1.0
CD2 B:HIS110 3.0 25.4 1.0
CG B:ASP109 3.1 34.6 1.0
CE1 B:HIS246 3.1 24.9 1.0
CD2 B:HIS246 3.2 29.1 1.0
CE1 B:HIS110 3.3 27.9 1.0
OD1 B:ASP109 3.3 30.9 1.0
ZN B:ZN300 3.4 30.3 0.8
C1 B:EDO302 3.8 65.4 1.0
O2 B:EDO302 4.0 48.7 1.0
NE2 B:HIS105 4.1 30.9 1.0
CE1 B:HIS105 4.2 27.8 1.0
O B:HOH485 4.2 37.2 1.0
CG B:HIS110 4.2 24.4 1.0
C2 B:EDO302 4.2 60.2 1.0
ND1 B:HIS246 4.3 26.8 1.0
ND1 B:HIS110 4.3 24.4 1.0
CG B:HIS246 4.3 26.4 1.0
CB B:ASP109 4.4 24.6 1.0
OG B:SER206 4.6 38.9 1.0
NE2 B:HIS181 4.7 25.0 1.0

Zinc binding site 5 out of 8 in 6u0y

Go back to Zinc Binding Sites List in 6u0y
Zinc binding site 5 out of 8 in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn301

b:34.9
occ:0.75
O C:HOH406 2.0 38.4 1.0
ND1 C:HIS107 2.1 33.5 1.0
NE2 C:HIS181 2.1 32.9 1.0
NE2 C:HIS105 2.3 36.4 1.0
O C:HOH568 2.6 45.5 1.0
CE1 C:HIS107 3.0 31.7 1.0
O C:HOH560 3.0 41.6 1.0
CD2 C:HIS181 3.1 29.3 1.0
CE1 C:HIS181 3.1 31.8 1.0
CG C:HIS107 3.1 27.4 1.0
CE1 C:HIS105 3.2 37.6 1.0
CD2 C:HIS105 3.2 34.2 1.0
ZN C:ZN302 3.5 44.8 0.6
CB C:HIS107 3.5 25.4 1.0
O C:HOH562 4.0 50.6 1.0
NE2 C:HIS107 4.1 28.5 1.0
OD1 C:ASP109 4.1 37.4 1.0
ND1 C:HIS181 4.2 28.2 1.0
CD2 C:HIS107 4.2 31.6 1.0
CG C:HIS181 4.2 27.4 1.0
ND1 C:HIS105 4.3 38.4 1.0
CG C:HIS105 4.3 32.9 1.0
CD2 C:HIS110 4.3 34.4 1.0
NE2 C:HIS110 4.5 32.6 1.0
O C:HOH468 4.7 44.4 1.0
OD2 C:ASP109 4.8 40.4 1.0
CG C:ASP109 5.0 33.6 1.0
CA C:HIS107 5.0 25.6 1.0

Zinc binding site 6 out of 8 in 6u0y

Go back to Zinc Binding Sites List in 6u0y
Zinc binding site 6 out of 8 in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn302

b:44.8
occ:0.58
O C:HOH560 2.0 41.6 1.0
O C:HOH562 2.2 50.6 1.0
NE2 C:HIS110 2.2 32.6 1.0
OD2 C:ASP109 2.3 40.4 1.0
NE2 C:HIS246 2.4 40.3 1.0
O C:HOH406 2.6 38.4 1.0
CG C:ASP109 3.1 33.6 1.0
CD2 C:HIS110 3.1 34.4 1.0
CE1 C:HIS110 3.2 37.8 1.0
OD1 C:ASP109 3.3 37.4 1.0
CE1 C:HIS246 3.4 36.4 1.0
CD2 C:HIS246 3.4 38.9 1.0
ZN C:ZN301 3.5 34.9 0.8
O C:HOH468 3.9 44.4 1.0
O C:HOH568 4.0 45.5 1.0
NE2 C:HIS105 4.2 36.4 1.0
CE1 C:HIS105 4.2 37.6 1.0
CG C:HIS110 4.3 31.6 1.0
ND1 C:HIS110 4.3 31.6 1.0
CB C:ASP109 4.5 31.0 1.0
ND1 C:HIS246 4.5 39.0 1.0
CG C:HIS246 4.5 37.8 1.0
NE2 C:HIS181 4.6 32.9 1.0

Zinc binding site 7 out of 8 in 6u0y

Go back to Zinc Binding Sites List in 6u0y
Zinc binding site 7 out of 8 in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn300

b:36.8
occ:0.72
O2 D:EDO302 1.9 38.8 1.0
ND1 D:HIS107 2.1 35.7 1.0
NE2 D:HIS181 2.2 37.2 1.0
NE2 D:HIS105 2.3 38.8 1.0
O1 D:EDO302 2.4 48.0 1.0
C2 D:EDO302 3.0 49.3 1.0
CE1 D:HIS107 3.1 35.5 1.0
CG D:HIS107 3.1 30.8 1.0
CD2 D:HIS181 3.2 31.9 1.0
CE1 D:HIS105 3.2 40.9 1.0
CD2 D:HIS105 3.2 36.5 1.0
CE1 D:HIS181 3.3 35.8 1.0
C1 D:EDO302 3.3 46.4 1.0
ZN D:ZN301 3.4 71.6 0.7
CB D:HIS107 3.4 31.9 1.0
OD1 D:ASP109 4.2 35.3 1.0
NE2 D:HIS107 4.2 31.9 1.0
CD2 D:HIS107 4.2 32.6 1.0
ND1 D:HIS105 4.3 39.0 1.0
CD2 D:HIS110 4.3 41.3 1.0
CG D:HIS181 4.3 33.8 1.0
CG D:HIS105 4.3 33.0 1.0
ND1 D:HIS181 4.3 32.5 1.0
NE2 D:HIS110 4.5 45.2 1.0
OD2 D:ASP109 4.9 45.6 1.0
CA D:HIS107 4.9 29.2 1.0
CG D:ASP109 5.0 37.9 1.0

Zinc binding site 8 out of 8 in 6u0y

Go back to Zinc Binding Sites List in 6u0y
Zinc binding site 8 out of 8 in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn301

b:71.6
occ:0.68
NE2 D:HIS110 2.3 45.2 1.0
NE2 D:HIS246 2.3 41.5 1.0
OD2 D:ASP109 2.3 45.6 1.0
O2 D:EDO302 2.6 38.8 1.0
CD2 D:HIS110 3.1 41.3 1.0
CG D:ASP109 3.1 37.9 1.0
OD1 D:ASP109 3.1 35.3 1.0
CD2 D:HIS246 3.3 41.3 1.0
CE1 D:HIS246 3.3 42.5 1.0
CE1 D:HIS110 3.3 43.5 1.0
ZN D:ZN300 3.4 36.8 0.7
C2 D:EDO302 3.5 49.3 1.0
C1 D:EDO302 4.1 46.4 1.0
NE2 D:HIS105 4.2 38.8 1.0
O1 D:EDO302 4.2 48.0 1.0
CE1 D:HIS105 4.3 40.9 1.0
CG D:HIS110 4.3 39.5 1.0
ND1 D:HIS110 4.3 41.3 1.0
ND1 D:HIS246 4.4 45.2 1.0
CG D:HIS246 4.4 39.0 1.0
CB D:ASP109 4.5 32.3 1.0
NE2 D:HIS181 4.7 37.2 1.0

Reference:

Y.Kim, N.Maltseva, M.Endres, A.Joachimiak, Center For Structural Genomics Of Infectious Diseases(Csgid). Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia To Be Published.
Page generated: Wed Dec 16 12:56:44 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy