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Zinc in PDB 2nyp: Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221D Doble Mutant with Two Zinc Ions.

Enzymatic activity of Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221D Doble Mutant with Two Zinc Ions.

All present enzymatic activity of Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221D Doble Mutant with Two Zinc Ions.:
3.5.2.6;

Protein crystallography data

The structure of Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221D Doble Mutant with Two Zinc Ions., PDB code: 2nyp was solved by F.J.Medrano Martin, A.J.Vila, J.M.Gonzalez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 68.68 / 1.84
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 52.464, 61.023, 68.710, 90.00, 92.92, 90.00
R / Rfree (%) 17.9 / 24.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221D Doble Mutant with Two Zinc Ions. (pdb code 2nyp). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221D Doble Mutant with Two Zinc Ions., PDB code: 2nyp:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2nyp

Go back to Zinc Binding Sites List in 2nyp
Zinc binding site 1 out of 2 in the Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221D Doble Mutant with Two Zinc Ions.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221D Doble Mutant with Two Zinc Ions. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:22.8
occ:1.00
NE2 A:HIS149 2.1 14.8 1.0
ND1 A:HIS88 2.1 16.6 1.0
NE2 A:HIS86 2.1 14.2 1.0
O A:HOH432 2.5 22.5 1.0
O A:HOH417 2.7 35.1 1.0
CD2 A:HIS149 2.9 12.4 1.0
CG A:HIS88 3.0 17.4 1.0
CD2 A:HIS86 3.1 14.0 1.0
CE1 A:HIS88 3.1 14.9 1.0
CE1 A:HIS86 3.1 16.7 1.0
CE1 A:HIS149 3.2 16.6 1.0
CB A:HIS88 3.3 18.7 1.0
OD1 A:ASP168 3.6 23.3 1.0
OD1 A:ASP90 4.0 34.6 1.0
CG A:HIS149 4.1 13.4 1.0
CG2 A:THR150 4.2 10.5 1.0
NE2 A:HIS88 4.2 17.9 1.0
CD2 A:HIS88 4.2 17.8 1.0
O A:HOH512 4.2 54.7 1.0
ND1 A:HIS149 4.2 12.5 1.0
ND1 A:HIS86 4.2 17.6 1.0
CG A:HIS86 4.2 14.1 1.0
CG A:ASP168 4.2 19.5 1.0
CB A:ASP168 4.4 14.4 1.0
CD2 A:HIS91 4.6 20.1 1.0
ZN A:ZN302 4.7 42.9 1.0
OD2 A:ASP90 4.7 36.3 1.0
CA A:HIS88 4.8 18.6 1.0
CG A:ASP90 4.8 30.3 1.0
NE2 A:HIS91 4.9 25.9 1.0
O A:HOH533 5.0 30.8 1.0

Zinc binding site 2 out of 2 in 2nyp

Go back to Zinc Binding Sites List in 2nyp
Zinc binding site 2 out of 2 in the Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221D Doble Mutant with Two Zinc Ions.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221D Doble Mutant with Two Zinc Ions. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:42.9
occ:1.00
NE2 A:HIS91 2.0 25.9 1.0
OD1 A:ASP168 2.2 23.3 1.0
O A:HOH417 2.5 35.1 1.0
O A:HOH463 2.7 33.9 1.0
CG A:ASP168 2.9 19.5 1.0
CD2 A:HIS91 2.9 20.1 1.0
OD2 A:ASP90 3.0 36.3 1.0
OD2 A:ASP168 3.0 27.2 1.0
CE1 A:HIS91 3.1 21.4 1.0
NE2 A:HIS210 3.2 34.2 1.0
CE1 A:HIS210 3.7 33.3 1.0
CG A:ASP90 3.8 30.3 1.0
OD1 A:ASP90 4.1 34.6 1.0
CG A:HIS91 4.1 22.9 1.0
CE1 A:HIS86 4.1 16.7 1.0
ND1 A:HIS91 4.1 24.1 1.0
O A:HOH512 4.2 54.7 1.0
CD2 A:HIS210 4.2 31.1 1.0
OG A:SER41 4.2 35.7 1.0
O A:HOH431 4.3 33.4 1.0
CB A:ASP168 4.3 14.4 1.0
O A:GLY209 4.6 17.4 1.0
NE2 A:HIS86 4.7 14.2 1.0
ND1 A:HIS210 4.7 32.4 1.0
ZN A:ZN301 4.7 22.8 1.0
CA A:GLY209 4.9 17.5 1.0
CB A:ASP90 4.9 26.1 1.0
C A:GLY209 5.0 18.6 1.0
CB A:SER41 5.0 32.3 1.0

Reference:

J.M.Gonzalez, F.J.Medrano Martin, A.L.Costello, D.L.Tierney, A.J.Vila. The ZN2 Position in Metallo-Beta-Lactamases Is Critical For Activity: A Study on Chimeric Metal Sites on A Conserved Protein Scaffold. J.Mol.Biol. V. 373 1141 2007.
ISSN: ISSN 0022-2836
PubMed: 17915249
DOI: 10.1016/J.JMB.2007.08.031
Page generated: Wed Dec 16 03:44:51 2020

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