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Zinc in PDB 2uyx: Metallo-Beta-Lactamase (1BC2) Single Point Mutant D120S

Enzymatic activity of Metallo-Beta-Lactamase (1BC2) Single Point Mutant D120S

All present enzymatic activity of Metallo-Beta-Lactamase (1BC2) Single Point Mutant D120S:
3.5.2.6;

Protein crystallography data

The structure of Metallo-Beta-Lactamase (1BC2) Single Point Mutant D120S, PDB code: 2uyx was solved by L.I.Larrull, S.M.Fabiane, J.M.Kowalski, B.Bennett, B.J.Sutton, A.J.Vila, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.01 / 1.95
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 53.389, 61.970, 69.573, 90.00, 93.28, 90.00
R / Rfree (%) 14.6 / 22.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Metallo-Beta-Lactamase (1BC2) Single Point Mutant D120S (pdb code 2uyx). 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 (1BC2) Single Point Mutant D120S, PDB code: 2uyx:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2uyx

Go back to Zinc Binding Sites List in 2uyx
Zinc binding site 1 out of 2 in the Metallo-Beta-Lactamase (1BC2) Single Point Mutant D120S


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 (1BC2) Single Point Mutant D120S within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1296

b:18.7
occ:1.00
NE2 A:HIS196 2.0 21.8 1.0
ND1 A:HIS118 2.0 23.4 1.0
NE2 A:HIS116 2.2 18.6 1.0
O A:HOH2281 2.2 30.1 0.5
O3 A:GOL1293 2.6 31.8 0.5
O3 A:GOL1292 2.9 20.9 0.5
CG A:HIS118 3.0 23.3 1.0
CD2 A:HIS196 3.0 22.6 1.0
CE1 A:HIS196 3.0 22.3 1.0
CE1 A:HIS118 3.0 24.2 1.0
CD2 A:HIS116 3.1 21.3 1.0
C3 A:GOL1292 3.1 22.5 0.5
CE1 A:HIS116 3.2 20.4 1.0
C3 A:GOL1293 3.2 30.4 0.5
CB A:HIS118 3.3 25.2 1.0
C1 A:GOL1292 4.0 26.9 0.5
O A:HOH2280 4.0 29.2 0.5
SG A:CYS221 4.1 33.4 1.0
ND1 A:HIS196 4.1 20.4 1.0
CD2 A:HIS118 4.1 23.6 1.0
NE2 A:HIS118 4.1 24.8 1.0
CG A:HIS196 4.1 22.6 1.0
C2 A:GOL1292 4.2 25.7 0.5
ND1 A:HIS116 4.2 21.1 1.0
ZN A:ZN1297 4.2 25.4 0.5
CG A:HIS116 4.2 23.2 1.0
C2 A:GOL1293 4.3 31.4 0.5
C1 A:GOL1293 4.3 31.3 0.5
CB A:CYS221 4.3 28.0 1.0
CG2 A:THR197 4.4 22.6 1.0
O1 A:GOL1292 4.7 28.5 0.5
OG A:SER120 4.7 32.5 1.0
CA A:HIS118 4.7 25.2 1.0
O2 A:GOL1293 4.8 32.9 0.5
O A:HOH2279 4.8 47.1 1.0

Zinc binding site 2 out of 2 in 2uyx

Go back to Zinc Binding Sites List in 2uyx
Zinc binding site 2 out of 2 in the Metallo-Beta-Lactamase (1BC2) Single Point Mutant D120S


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 (1BC2) Single Point Mutant D120S within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1297

b:25.4
occ:0.50
NE2 A:HIS263 2.1 36.3 1.0
O A:HOH2280 2.2 29.2 0.5
SG A:CYS221 2.2 33.4 1.0
O A:HOH2283 2.3 10.4 0.5
CD2 A:HIS263 2.8 35.9 1.0
O3 A:GOL1293 2.9 31.8 0.5
C3 A:GOL1292 2.9 22.5 0.5
CB A:CYS221 3.2 28.0 1.0
CE1 A:HIS263 3.3 35.5 1.0
O A:HOH2281 3.3 30.1 0.5
C3 A:GOL1293 3.3 30.4 0.5
O A:HOH2199 3.5 33.3 0.5
O A:HOH2275 3.9 42.9 1.0
O3 A:GOL1292 3.9 20.9 0.5
NH2 A:ARG121 3.9 35.1 1.0
C2 A:GOL1292 3.9 25.7 0.5
CG A:HIS263 4.0 31.9 1.0
ND1 A:HIS263 4.2 34.4 1.0
ZN A:ZN1296 4.2 18.7 1.0
NE2 A:HIS196 4.2 21.8 1.0
CE1 A:HIS196 4.3 22.3 1.0
CA A:CYS221 4.3 27.2 1.0
C2 A:GOL1293 4.6 31.4 0.5
OG A:SER120 4.6 32.5 1.0
C1 A:GOL1292 4.8 26.9 0.5
CZ A:ARG121 4.9 32.9 1.0
O2 A:GOL1292 4.9 27.1 0.5
O A:HOH2001 4.9 39.0 1.0
O A:HOH2198 4.9 17.5 1.0
NE A:ARG121 4.9 33.2 1.0
ND1 A:HIS196 5.0 20.4 1.0

Reference:

L.I.Llarrull, S.M.Fabiane, J.M.Kowalski, B.Bennett, B.J.Sutton, A.J.Vila. Asp-120 Locates ZN2 For Optimal Metallo-Beta-Lactamase Activity. J. Biol. Chem. V. 282 18276 2007.
ISSN: ISSN 0021-9258
PubMed: 17426028
DOI: 10.1074/JBC.M700742200
Page generated: Sat Sep 26 03:58:21 2020
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