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Zinc in PDB 6v71: Crystal Structure of Metallo Beta Lactamase From Hirschia Baltica with Nitrate in the Active Site

Enzymatic activity of Crystal Structure of Metallo Beta Lactamase From Hirschia Baltica with Nitrate in the Active Site

All present enzymatic activity of Crystal Structure of Metallo Beta Lactamase From Hirschia Baltica with Nitrate in the Active Site:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of Metallo Beta Lactamase From Hirschia Baltica with Nitrate in the Active Site, PDB code: 6v71 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) 38.68 / 1.40
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 77.362, 77.362, 241.321, 90.00, 90.00, 120.00
R / Rfree (%) 14.3 / 16.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Metallo Beta Lactamase From Hirschia Baltica with Nitrate in the Active Site (pdb code 6v71). 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 with Nitrate in the Active Site, PDB code: 6v71:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 6v71

Go back to Zinc Binding Sites List in 6v71
Zinc binding site 1 out of 2 in the Crystal Structure of Metallo Beta Lactamase From Hirschia Baltica with Nitrate in the Active Site


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 with Nitrate in the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:19.7
occ:1.00
O A:HOH431 2.0 19.8 1.0
NE2 A:HIS241 2.1 17.9 1.0
OD2 A:ASP120 2.1 20.2 1.0
SG A:CYS199 2.3 18.4 1.0
O1 A:NO3304 2.3 21.3 1.0
CE1 A:HIS241 3.0 18.6 1.0
CD2 A:HIS241 3.1 19.1 1.0
CG A:ASP120 3.1 18.5 1.0
N A:NO3304 3.1 22.8 1.0
O2 A:NO3304 3.1 26.5 1.0
CB A:CYS199 3.4 17.6 1.0
OD1 A:ASP120 3.4 20.8 1.0
ZN A:ZN302 3.5 18.8 1.0
O A:HOH501 4.1 29.2 1.0
ND1 A:HIS241 4.2 19.7 1.0
NE2 A:HIS180 4.2 17.1 1.0
CG A:HIS241 4.2 18.4 1.0
O3 A:NO3304 4.3 25.4 1.0
CE1 A:HIS180 4.4 18.4 1.0
CB A:ASP120 4.4 18.6 1.0
CE1 A:HIS116 4.4 18.7 1.0
NE2 A:HIS116 4.4 17.4 1.0
CB A:SER240 4.4 18.8 1.0
CA A:CYS199 4.6 18.0 1.0
OG A:SER240 4.7 18.4 1.0
O A:HOH458 4.7 20.9 1.0
CD2 A:HIS180 5.0 17.2 1.0

Zinc binding site 2 out of 2 in 6v71

Go back to Zinc Binding Sites List in 6v71
Zinc binding site 2 out of 2 in the Crystal Structure of Metallo Beta Lactamase From Hirschia Baltica with Nitrate in the Active Site


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 with Nitrate in the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:18.8
occ:1.00
O A:HOH431 2.0 19.8 1.0
ND1 A:HIS118 2.0 18.7 1.0
NE2 A:HIS180 2.0 17.1 1.0
NE2 A:HIS116 2.0 17.4 1.0
CE1 A:HIS118 3.0 18.9 1.0
CE1 A:HIS180 3.0 18.4 1.0
CD2 A:HIS180 3.0 17.2 1.0
CD2 A:HIS116 3.0 17.9 1.0
CE1 A:HIS116 3.0 18.7 1.0
CG A:HIS118 3.0 18.8 1.0
CB A:HIS118 3.4 18.1 1.0
ZN A:ZN301 3.5 19.7 1.0
O A:HOH501 3.8 29.2 1.0
O1 A:NO3304 3.9 21.3 1.0
OD1 A:ASP120 3.9 20.8 1.0
SG A:CYS199 4.0 18.4 1.0
NE2 A:HIS118 4.1 19.9 1.0
ND1 A:HIS180 4.1 19.6 1.0
ND1 A:HIS116 4.1 19.2 1.0
CG A:HIS180 4.1 19.1 1.0
CD2 A:HIS118 4.1 20.0 1.0
CG A:HIS116 4.1 17.6 1.0
CB A:CYS199 4.1 17.6 1.0
O2 A:NO3304 4.3 26.5 1.0
N A:NO3304 4.4 22.8 1.0
OD2 A:ASP120 4.5 20.2 1.0
CG A:ASP120 4.7 18.5 1.0
CA A:HIS118 4.8 18.5 1.0

Reference:

N.Maltseva, Y.Kim, S.Clancy, M.Endres, R.Mulligan, A.Joachimiak, Center For Structural Genomics Of Infectious Diseases(Csgid). Crystal Structure of Metallo Beta Lactamase From Hirschia Baltica with Nitrate in the Active Site To Be Published.
Page generated: Tue Oct 29 08:56:21 2024

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