Zinc in PDB 6v54: Crystal Structure of Metallo Beta Lactamase From Hirschia Baltica

Enzymatic activity of Crystal Structure of Metallo Beta Lactamase From Hirschia Baltica

All present enzymatic activity of Crystal Structure of Metallo Beta Lactamase From Hirschia Baltica:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of Metallo Beta Lactamase From Hirschia Baltica, PDB code: 6v54 was solved by N.Maltseva, Y.Kim, S.Clancy, M.Endres, R.Mulligan, A.Joachimiak, Center Forstructural Genomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.37 / 1.45
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 77.668, 77.668, 240.998, 90.00, 90.00, 120.00
R / Rfree (%) 13.2 / 16.3

Other elements in 6v54:

The structure of Crystal Structure of Metallo Beta Lactamase From Hirschia Baltica also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Metallo Beta Lactamase From Hirschia Baltica (pdb code 6v54). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Metallo Beta Lactamase From Hirschia Baltica, PDB code: 6v54:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 6v54

Go back to Zinc Binding Sites List in 6v54
Zinc binding site 1 out of 2 in the Crystal Structure of Metallo Beta Lactamase From Hirschia Baltica


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 Metallo Beta Lactamase From Hirschia Baltica within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn305

b:16.1
occ:0.97
NE2 A:HIS241 2.0 12.7 1.0
O A:HOH445 2.1 17.3 1.0
OD2 A:ASP120 2.1 17.2 1.0
SG A:CYS199 2.2 14.6 1.0
O1 A:FMT302 2.5 23.1 0.8
CE1 A:HIS241 3.0 15.2 1.0
CD2 A:HIS241 3.1 13.0 1.0
CG A:ASP120 3.1 14.8 1.0
C A:FMT302 3.4 23.3 0.8
OD1 A:ASP120 3.4 16.0 1.0
CB A:CYS199 3.4 12.7 1.0
ZN A:ZN306 3.5 12.3 0.8
O A:HOH514 4.0 30.1 1.0
ND1 A:HIS241 4.1 15.8 1.0
CG A:HIS241 4.2 12.4 1.0
NE2 A:HIS180 4.3 12.9 1.0
O2 A:FMT302 4.3 21.1 0.8
CB A:ASP120 4.4 14.5 1.0
CE1 A:HIS116 4.4 13.5 1.0
CB A:SER240 4.4 13.9 1.0
NE2 A:HIS116 4.5 13.0 1.0
CE1 A:HIS180 4.6 13.1 1.0
CA A:CYS199 4.6 12.5 1.0
OG A:SER240 4.7 15.9 1.0
O A:HOH441 4.8 16.6 1.0

Zinc binding site 2 out of 2 in 6v54

Go back to Zinc Binding Sites List in 6v54
Zinc binding site 2 out of 2 in the Crystal Structure of Metallo Beta Lactamase From Hirschia Baltica


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 Metallo Beta Lactamase From Hirschia Baltica within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn306

b:12.3
occ:0.84
O A:HOH445 1.9 17.3 1.0
ND1 A:HIS118 2.0 13.8 1.0
NE2 A:HIS180 2.0 12.9 1.0
NE2 A:HIS116 2.0 13.0 1.0
CE1 A:HIS116 3.0 13.5 1.0
CD2 A:HIS180 3.0 13.5 1.0
CG A:HIS118 3.0 13.8 1.0
CE1 A:HIS118 3.0 16.8 1.0
CE1 A:HIS180 3.0 13.1 1.0
CD2 A:HIS116 3.1 12.7 1.0
CB A:HIS118 3.3 12.8 1.0
ZN A:ZN305 3.5 16.1 1.0
O A:HOH514 3.7 30.1 1.0
O1 A:FMT302 3.8 23.1 0.8
OD1 A:ASP120 3.9 16.0 1.0
SG A:CYS199 4.0 14.6 1.0
ND1 A:HIS116 4.1 13.3 1.0
CB A:CYS199 4.1 12.7 1.0
NE2 A:HIS118 4.1 17.0 1.0
CG A:HIS180 4.1 11.7 1.0
CD2 A:HIS118 4.1 15.6 1.0
ND1 A:HIS180 4.1 13.9 1.0
CG A:HIS116 4.2 11.9 1.0
C A:FMT302 4.5 23.3 0.8
OD2 A:ASP120 4.6 17.2 1.0
CG A:ASP120 4.7 14.8 1.0
CA A:HIS118 4.8 11.8 1.0

Reference:

N.Maltseva, Y.Kim, S.Clancy, M.Endres, R.Mulligan, A.Joachimiak. Crystal Structure of Metallo Beta Lactamase From Hirschia Baltica. To Be Published.
Page generated: Wed Dec 16 13:00:50 2020

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