Atomistry » Zinc » PDB 2b8k-2bnm » 2bmi
Atomistry »
  Zinc »
    PDB 2b8k-2bnm »
      2bmi »

Zinc in PDB 2bmi: Metallo-Beta-Lactamase

Enzymatic activity of Metallo-Beta-Lactamase

All present enzymatic activity of Metallo-Beta-Lactamase:
3.5.2.6;

Protein crystallography data

The structure of Metallo-Beta-Lactamase, PDB code: 2bmi was solved by A.Carfi, E.Duee, O.Dideberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.256, 94.920, 111.420, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 26.2

Other elements in 2bmi:

The structure of Metallo-Beta-Lactamase also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Metallo-Beta-Lactamase (pdb code 2bmi). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Metallo-Beta-Lactamase, PDB code: 2bmi:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 2bmi

Go back to Zinc Binding Sites List in 2bmi
Zinc binding site 1 out of 4 in the Metallo-Beta-Lactamase


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn271

b:12.1
occ:1.00
O A:HOH276 1.8 6.8 1.0
NE2 A:HIS145 2.1 9.3 1.0
ND1 A:HIS84 2.1 7.5 1.0
NE2 A:HIS82 2.1 10.0 1.0
CD2 A:HIS145 3.0 10.2 1.0
CG A:HIS84 3.0 4.5 1.0
CE1 A:HIS82 3.0 7.8 1.0
CE1 A:HIS84 3.1 7.9 1.0
CE1 A:HIS145 3.1 11.4 1.0
CD2 A:HIS82 3.2 5.2 1.0
CB A:HIS84 3.3 6.1 1.0
ZN A:ZN272 3.4 10.0 1.0
O A:HOH410 3.5 25.2 1.0
O A:HOH492 3.9 9.7 1.0
OD1 A:ASP86 3.9 7.6 1.0
CG A:HIS145 4.2 11.9 1.0
CD2 A:HIS84 4.2 2.0 1.0
ND1 A:HIS82 4.2 7.8 1.0
SG A:CYS164 4.2 8.2 1.0
NE2 A:HIS84 4.2 4.2 1.0
ND1 A:HIS145 4.2 10.5 1.0
OD2 A:ASP86 4.3 6.1 1.0
CB A:CYS164 4.3 9.9 1.0
CG A:HIS82 4.3 7.8 1.0
CG A:ASP86 4.5 8.2 1.0
CA A:HIS84 4.8 9.0 1.0

Zinc binding site 2 out of 4 in 2bmi

Go back to Zinc Binding Sites List in 2bmi
Zinc binding site 2 out of 4 in the Metallo-Beta-Lactamase


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn272

b:10.0
occ:1.00
O A:HOH276 1.9 6.8 1.0
NE2 A:HIS206 2.0 3.3 1.0
OD2 A:ASP86 2.2 6.1 1.0
O A:HOH492 2.2 9.7 1.0
SG A:CYS164 2.4 8.2 1.0
CD2 A:HIS206 3.0 2.4 1.0
CE1 A:HIS206 3.0 3.6 1.0
CG A:ASP86 3.2 8.2 1.0
ZN A:ZN271 3.4 12.1 1.0
CB A:CYS164 3.5 9.9 1.0
OD1 A:ASP86 3.6 7.6 1.0
O A:HOH410 3.9 25.2 1.0
NE2 A:HIS145 4.0 9.3 1.0
O A:HOH493 4.0 9.0 1.0
ND1 A:HIS206 4.2 2.8 1.0
CG A:HIS206 4.2 3.4 1.0
CE1 A:HIS145 4.2 11.4 1.0
O A:HOH288 4.5 4.1 1.0
CB A:ASP86 4.5 7.8 1.0
CE1 A:HIS82 4.5 7.8 1.0
NE2 A:HIS82 4.6 10.0 1.0
CA A:CYS164 4.7 9.3 1.0
CD2 A:HIS145 4.8 10.2 1.0

Zinc binding site 3 out of 4 in 2bmi

Go back to Zinc Binding Sites List in 2bmi
Zinc binding site 3 out of 4 in the Metallo-Beta-Lactamase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Metallo-Beta-Lactamase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn271

b:11.2
occ:1.00
O B:HOH278 1.9 8.0 1.0
ND1 B:HIS84 2.1 8.4 1.0
NE2 B:HIS145 2.1 12.2 1.0
NE2 B:HIS82 2.1 5.8 1.0
CE1 B:HIS82 3.0 6.3 1.0
CD2 B:HIS145 3.0 8.5 1.0
CG B:HIS84 3.0 8.6 1.0
CE1 B:HIS84 3.1 7.0 1.0
CE1 B:HIS145 3.1 12.8 1.0
CD2 B:HIS82 3.2 7.7 1.0
CB B:HIS84 3.3 9.4 1.0
ZN B:ZN272 3.5 12.2 1.0
O B:HOH406 3.6 15.6 1.0
O B:HOH474 3.8 11.5 1.0
OD1 B:ASP86 4.0 8.8 1.0
ND1 B:HIS82 4.2 5.0 1.0
CG B:HIS145 4.2 8.7 1.0
CD2 B:HIS84 4.2 6.6 1.0
NE2 B:HIS84 4.2 9.2 1.0
ND1 B:HIS145 4.2 8.9 1.0
SG B:CYS164 4.2 8.9 1.0
OD2 B:ASP86 4.2 8.3 1.0
CB B:CYS164 4.3 5.8 1.0
CG B:HIS82 4.3 5.6 1.0
CG B:ASP86 4.6 9.4 1.0
CA B:HIS84 4.8 10.2 1.0

Zinc binding site 4 out of 4 in 2bmi

Go back to Zinc Binding Sites List in 2bmi
Zinc binding site 4 out of 4 in the Metallo-Beta-Lactamase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Metallo-Beta-Lactamase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn272

b:12.2
occ:1.00
O B:HOH278 1.9 8.0 1.0
NE2 B:HIS206 2.1 8.6 1.0
OD2 B:ASP86 2.1 8.3 1.0
O B:HOH474 2.2 11.5 1.0
SG B:CYS164 2.4 8.9 1.0
CD2 B:HIS206 3.0 9.6 1.0
CE1 B:HIS206 3.2 8.0 1.0
CG B:ASP86 3.2 9.4 1.0
ZN B:ZN271 3.5 11.2 1.0
CB B:CYS164 3.5 5.8 1.0
OD1 B:ASP86 3.6 8.8 1.0
O B:HOH475 4.0 8.1 1.0
CG B:HIS206 4.2 7.1 1.0
O B:HOH406 4.2 15.6 1.0
ND1 B:HIS206 4.2 7.2 1.0
NE2 B:HIS145 4.3 12.2 1.0
CB B:ASP86 4.5 6.7 1.0
CE1 B:HIS145 4.5 12.8 1.0
CE1 B:HIS82 4.5 6.3 1.0
O B:HOH291 4.5 6.3 1.0
NE2 B:HIS82 4.6 5.8 1.0
CA B:CYS164 4.7 9.0 1.0
O B:GLY205 4.9 8.7 1.0
CD2 B:HIS145 5.0 8.5 1.0

Reference:

A.Carfi, E.Duee, R.Paul-Soto, M.Galleni, J.M.Frere, O.Dideberg. X-Ray Structure of the Znii Beta-Lactamase From Bacteroides Fragilis in An Orthorhombic Crystal Form. Acta Crystallogr.,Sect.D V. 54 45 1998.
ISSN: ISSN 0907-4449
PubMed: 9761816
DOI: 10.1107/S090744499700927X
Page generated: Wed Oct 16 22:03:36 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy