Atomistry » Zinc » PDB 6dit-6dxq » 6dqh
Atomistry »
  Zinc »
    PDB 6dit-6dxq »
      6dqh »

Zinc in PDB 6dqh: Cronobacter Sakazakii (Enterobacter Sakazakii) Metallo-Beta-Lactamse Harldq Motif

Protein crystallography data

The structure of Cronobacter Sakazakii (Enterobacter Sakazakii) Metallo-Beta-Lactamse Harldq Motif, PDB code: 6dqh was solved by M.Monteiro Pedroso, D.Waite, M.Natasa, R.Mcgeary, L.Guddat, P.Hugenholtz, G.Schenk, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.28 / 1.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.768, 68.601, 76.246, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / 19.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Cronobacter Sakazakii (Enterobacter Sakazakii) Metallo-Beta-Lactamse Harldq Motif (pdb code 6dqh). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Cronobacter Sakazakii (Enterobacter Sakazakii) Metallo-Beta-Lactamse Harldq Motif, PDB code: 6dqh:

Zinc binding site 1 out of 1 in 6dqh

Go back to Zinc Binding Sites List in 6dqh
Zinc binding site 1 out of 1 in the Cronobacter Sakazakii (Enterobacter Sakazakii) Metallo-Beta-Lactamse Harldq Motif


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cronobacter Sakazakii (Enterobacter Sakazakii) Metallo-Beta-Lactamse Harldq Motif within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:8.8
occ:1.00
O A:HOH526 2.0 14.2 1.0
NE2 A:HIS192 2.1 8.2 1.0
ND1 A:HIS118 2.1 7.3 1.0
NE2 A:HIS116 2.1 8.3 1.0
O2 A:PO4405 2.3 13.9 0.9
O A:HOH525 2.5 25.4 1.0
CE1 A:HIS118 3.0 9.4 1.0
CE1 A:HIS116 3.0 7.8 1.0
CD2 A:HIS192 3.0 7.3 1.0
CD2 A:HIS116 3.0 6.4 1.0
HB2 A:HIS118 3.1 9.2 1.0
CE1 A:HIS192 3.1 9.1 1.0
CG A:HIS118 3.1 8.2 1.0
HE1 A:HIS118 3.1 11.3 1.0
HD2 A:HIS192 3.2 8.7 1.0
HE1 A:HIS116 3.2 9.3 1.0
HD2 A:HIS116 3.2 7.7 1.0
HE1 A:HIS192 3.3 10.9 1.0
P A:PO4405 3.5 10.6 0.9
CB A:HIS118 3.5 7.7 1.0
O1 A:PO4405 3.5 12.4 0.9
HB3 A:HIS118 3.7 9.2 1.0
ND1 A:HIS116 4.1 7.9 1.0
CG A:HIS116 4.1 6.8 1.0
NE2 A:HIS118 4.1 8.4 1.0
ND1 A:HIS192 4.2 7.9 1.0
CG A:HIS192 4.2 7.2 1.0
CD2 A:HIS118 4.2 9.2 1.0
O4 A:PO4405 4.3 11.2 0.9
OD1 A:ASP120 4.3 10.0 1.0
HG2 A:GLN121 4.5 11.9 1.0
HG A:SER214 4.5 10.0 1.0
O3 A:PO4405 4.6 15.6 0.9
HB3 A:SER214 4.6 10.6 1.0
HG3 A:GLN121 4.7 11.9 1.0
HZ3 A:LYS260 4.8 17.5 1.0
HD1 A:HIS116 4.8 9.5 1.0
HB2 A:SER214 4.9 10.6 1.0
HG A:LEU193 4.9 9.3 1.0
HD21 A:ASN259 4.9 14.2 1.0
HE2 A:HIS118 4.9 10.1 1.0
HD1 A:HIS192 4.9 9.5 1.0
CA A:HIS118 4.9 6.9 1.0
HZ2 A:LYS260 5.0 17.5 1.0

Reference:

M.Monteiro Pedroso, D.Waite, M.Natasa, R.Mcgeary, L.Guddat, P.Hugenholtz, G.Schenk. Evolution and Diversity of B3-Type Metallo-Beta-Lactamases, Emerging Contributors to the Spread of Antibiotic Resistance. To Be Published.
Page generated: Mon Oct 28 19:43:37 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy