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Zinc in PDB 2bc2: Metallo Beta-Lactamase II From Bacillus Cereus 569/H/9 at pH 6.0, Trigonal Crystal Form

Enzymatic activity of Metallo Beta-Lactamase II From Bacillus Cereus 569/H/9 at pH 6.0, Trigonal Crystal Form

All present enzymatic activity of Metallo Beta-Lactamase II From Bacillus Cereus 569/H/9 at pH 6.0, Trigonal Crystal Form:
3.5.2.6;

Protein crystallography data

The structure of Metallo Beta-Lactamase II From Bacillus Cereus 569/H/9 at pH 6.0, Trigonal Crystal Form, PDB code: 2bc2 was solved by S.M.Fabiane, B.J.Sutton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.70
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 67.320, 67.320, 177.900, 90.00, 90.00, 120.00
R / Rfree (%) 20 / 25.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Metallo Beta-Lactamase II From Bacillus Cereus 569/H/9 at pH 6.0, Trigonal Crystal Form (pdb code 2bc2). 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 II From Bacillus Cereus 569/H/9 at pH 6.0, Trigonal Crystal Form, PDB code: 2bc2:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2bc2

Go back to Zinc Binding Sites List in 2bc2
Zinc binding site 1 out of 2 in the Metallo Beta-Lactamase II From Bacillus Cereus 569/H/9 at pH 6.0, Trigonal Crystal Form


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 II From Bacillus Cereus 569/H/9 at pH 6.0, Trigonal Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn228

b:20.2
occ:1.00
ND1 A:HIS88 2.0 21.2 1.0
NE2 A:HIS149 2.1 17.9 1.0
O A:HOH232 2.1 22.3 1.0
NE2 A:HIS86 2.3 15.0 1.0
O A:HOH380 2.7 33.7 1.0
CG A:HIS88 2.9 21.4 1.0
CE1 A:HIS88 3.0 20.7 1.0
CD2 A:HIS149 3.0 14.7 1.0
CE1 A:HIS149 3.1 18.6 1.0
CD2 A:HIS86 3.1 15.9 1.0
CB A:HIS88 3.3 18.5 1.0
CE1 A:HIS86 3.3 15.6 1.0
OD1 A:CSD168 3.7 22.9 1.0
NE2 A:HIS88 4.1 22.6 1.0
CD2 A:HIS88 4.1 20.5 1.0
CG A:HIS149 4.2 16.0 1.0
ND1 A:HIS149 4.2 16.4 1.0
OD1 A:ASP90 4.2 24.9 1.0
O A:HOH543 4.3 71.5 1.0
CG A:HIS86 4.3 15.3 1.0
CG2 A:THR150 4.3 13.4 1.0
ND1 A:HIS86 4.3 16.1 1.0
SG A:CSD168 4.6 21.2 1.0
CB A:CSD168 4.7 17.9 1.0
CA A:HIS88 4.7 19.2 1.0
O A:HOH300 4.8 20.2 1.0
OD2 A:ASP90 5.0 26.3 1.0

Zinc binding site 2 out of 2 in 2bc2

Go back to Zinc Binding Sites List in 2bc2
Zinc binding site 2 out of 2 in the Metallo Beta-Lactamase II From Bacillus Cereus 569/H/9 at pH 6.0, Trigonal Crystal Form


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 II From Bacillus Cereus 569/H/9 at pH 6.0, Trigonal Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn228

b:21.3
occ:1.00
NE2 B:HIS149 2.0 14.9 1.0
ND1 B:HIS88 2.1 18.1 1.0
O B:HOH231 2.2 23.3 1.0
NE2 B:HIS86 2.2 15.9 1.0
O B:HOH378 2.6 27.1 1.0
CE1 B:HIS149 3.0 14.7 1.0
CD2 B:HIS149 3.0 15.4 1.0
CG B:HIS88 3.0 17.6 1.0
CE1 B:HIS88 3.1 18.0 1.0
CE1 B:HIS86 3.1 16.4 1.0
CD2 B:HIS86 3.2 15.3 1.0
CB B:HIS88 3.3 18.7 1.0
OD1 B:CSD168 3.5 21.8 1.0
ND1 B:HIS149 4.1 15.4 1.0
CG B:HIS149 4.1 14.2 1.0
NE2 B:HIS88 4.1 20.5 1.0
CD2 B:HIS88 4.2 16.8 1.0
ND1 B:HIS86 4.2 16.0 1.0
OD1 B:ASP90 4.3 24.7 1.0
CG B:HIS86 4.3 15.3 1.0
CG2 B:THR150 4.4 13.7 1.0
SG B:CSD168 4.5 20.1 1.0
O B:HOH414 4.6 40.0 1.0
CB B:CSD168 4.6 18.2 1.0
CA B:HIS88 4.8 17.4 1.0
OD2 B:ASP90 4.9 23.7 1.0
O B:HOH357 5.0 28.5 1.0

Reference:

S.M.Fabiane, M.K.Sohi, B.J.Sutton. Null To Be Published.
Page generated: Wed Dec 16 03:18:18 2020

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