Atomistry » Zinc » PDB 2q1z-2ql1 » 2qdt
Atomistry »
  Zinc »
    PDB 2q1z-2ql1 »
      2qdt »

Zinc in PDB 2qdt: Structural Basis For the Broad-Spectrum Inhibition of Metallo-{Beta}- Lactamases: L1- IS38 Complex

Enzymatic activity of Structural Basis For the Broad-Spectrum Inhibition of Metallo-{Beta}- Lactamases: L1- IS38 Complex

All present enzymatic activity of Structural Basis For the Broad-Spectrum Inhibition of Metallo-{Beta}- Lactamases: L1- IS38 Complex:
3.5.2.6;

Protein crystallography data

The structure of Structural Basis For the Broad-Spectrum Inhibition of Metallo-{Beta}- Lactamases: L1- IS38 Complex, PDB code: 2qdt was solved by G.Garau, O.Dideberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.54 / 2.00
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 105.319, 105.319, 97.960, 90.00, 90.00, 120.00
R / Rfree (%) 17 / 19.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Structural Basis For the Broad-Spectrum Inhibition of Metallo-{Beta}- Lactamases: L1- IS38 Complex (pdb code 2qdt). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Structural Basis For the Broad-Spectrum Inhibition of Metallo-{Beta}- Lactamases: L1- IS38 Complex, PDB code: 2qdt:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 2qdt

Go back to Zinc Binding Sites List in 2qdt
Zinc binding site 1 out of 4 in the Structural Basis For the Broad-Spectrum Inhibition of Metallo-{Beta}- Lactamases: L1- IS38 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Basis For the Broad-Spectrum Inhibition of Metallo-{Beta}- Lactamases: L1- IS38 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:35.2
occ:1.00
 NE2 A:HIS160 2.0 30.3 1.0
NE2 A:HIS84 2.1 31.7 1.0
ND1 A:HIS86 2.1 33.2 1.0
S A:I38501 2.3 34.8 1.0
CD2 A:HIS160 2.9 30.5 1.0
CD2 A:HIS84 3.0 32.1 1.0
CE1 A:HIS86 3.0 33.5 1.0
CE1 A:HIS84 3.1 30.1 1.0
CE1 A:HIS160 3.1 30.0 1.0
C1 A:I38501 3.2 39.2 1.0
CG A:HIS86 3.2 33.5 1.0
CB A:HIS86 3.6 31.9 1.0
ZN A:ZN402 3.7 35.6 1.0
CG A:HIS160 4.1 31.5 1.0
CG A:HIS84 4.1 31.1 1.0
ND1 A:HIS84 4.1 30.2 1.0
ND1 A:HIS160 4.1 31.2 1.0
CD2 A:HIS89 4.2 34.2 1.0
NE2 A:HIS86 4.2 32.0 1.0
NE2 A:HIS89 4.3 34.6 1.0
CD2 A:HIS86 4.3 33.1 1.0
OD1 A:ASP88 4.3 32.0 1.0
C2 A:I38501 4.6 42.0 1.0
O A:HOH606 4.8 45.6 1.0
OG A:SER185 4.9 32.4 1.0
CE2 A:PHE124 4.9 35.9 1.0

Zinc binding site 2 out of 4 in 2qdt

Go back to Zinc Binding Sites List in 2qdt
Zinc binding site 2 out of 4 in the Structural Basis For the Broad-Spectrum Inhibition of Metallo-{Beta}- Lactamases: L1- IS38 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structural Basis For the Broad-Spectrum Inhibition of Metallo-{Beta}- Lactamases: L1- IS38 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn402

b:35.6
occ:1.00
 OD2 A:ASP88 2.0 32.7 1.0
NE2 A:HIS89 2.1 34.6 1.0
NE2 A:HIS225 2.1 32.6 1.0
S A:I38501 2.3 34.8 1.0
CG A:ASP88 2.7 33.0 1.0
OD1 A:ASP88 2.9 32.0 1.0
CE1 A:HIS89 2.9 34.4 1.0
CE1 A:HIS225 3.0 34.2 1.0
CD2 A:HIS89 3.0 34.2 1.0
CD2 A:HIS225 3.1 34.4 1.0
C1 A:I38501 3.2 39.2 1.0
C2 A:I38501 3.5 42.0 1.0
ZN A:ZN401 3.7 35.2 1.0
N4 A:I38501 3.9 51.0 1.0
ND1 A:HIS89 4.0 33.9 1.0
CG A:HIS89 4.1 33.4 1.0
ND1 A:HIS225 4.1 33.0 1.0
CB A:ASP88 4.2 32.5 1.0
C3 A:I38501 4.2 46.1 1.0
CG A:HIS225 4.2 34.6 1.0
O A:HOH606 4.2 45.6 1.0
NE2 A:HIS84 4.3 31.7 1.0
CE1 A:HIS84 4.5 30.1 1.0
O62 A:I38501 4.9 55.5 1.0
CZ3 A:TRP17 5.0 36.9 1.0
OG A:SER185 5.0 32.4 1.0

Zinc binding site 3 out of 4 in 2qdt

Go back to Zinc Binding Sites List in 2qdt
Zinc binding site 3 out of 4 in the Structural Basis For the Broad-Spectrum Inhibition of Metallo-{Beta}- Lactamases: L1- IS38 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structural Basis For the Broad-Spectrum Inhibition of Metallo-{Beta}- Lactamases: L1- IS38 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn403

b:98.9
occ:0.25
 ZN A:ZN403 0.0 98.9 0.2
NE2 A:HIS29 1.3 48.3 0.5
CE1 A:HIS29 1.3 47.1 0.5
NE2 A:HIS29 1.8 47.8 0.5
CE1 A:HIS29 2.1 47.1 0.5
CD2 A:HIS29 2.5 46.7 0.5
ND1 A:HIS29 2.6 46.2 0.5
CD2 A:HIS29 3.1 45.4 0.5
ND1 A:HIS29 3.3 45.9 0.5
CG A:HIS29 3.5 44.5 0.5
CG A:HIS29 3.5 44.7 0.5
ZN A:ZN403 3.6 0.0 0.3
CB A:HIS29 4.9 42.9 1.0

Zinc binding site 4 out of 4 in 2qdt

Go back to Zinc Binding Sites List in 2qdt
Zinc binding site 4 out of 4 in the Structural Basis For the Broad-Spectrum Inhibition of Metallo-{Beta}- Lactamases: L1- IS38 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structural Basis For the Broad-Spectrum Inhibition of Metallo-{Beta}- Lactamases: L1- IS38 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn403

b:0.0
occ:0.25
 ZN A:ZN403 0.0 0.0 0.3
ZN A:ZN403 3.6 98.9 0.2
CE1 A:HIS29 3.7 47.1 0.5
OD2 A:ASP28 4.0 45.3 1.0
NE2 A:HIS29 4.1 47.8 0.5
NE2 A:HIS29 4.2 48.3 0.5
OG1 A:THR172 4.3 49.6 1.0
CE1 A:HIS29 4.4 47.1 0.5
CB A:ASP28 4.6 42.1 1.0
CG A:ASP28 4.6 44.1 1.0
ND1 A:HIS29 4.8 45.9 0.5

Reference:

B.M.Lienard, G.Garau, L.Horsfall, A.I.Karsisiotis, C.Damblon, P.Lassaux, C.Papamicael, G.C.Roberts, M.Galleni, O.Dideberg, J.M.Frere, C.J.Schofield. Structural Basis For the Broad-Spectrum Inhibition of Metallo-Beta-Lactamases By Thiols. Org.Biomol.Chem. V. 6 2282 2008.
ISSN: ISSN 1477-0520
PubMed: 18563261
DOI: 10.1039/B802311E
Page generated: Thu Oct 17 03:23:51 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy