Atomistry » Zinc » PDB 4tph-4u4t » 4tyt
Atomistry »
  Zinc »
    PDB 4tph-4u4t »
      4tyt »

Zinc in PDB 4tyt: Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with ML302F

Enzymatic activity of Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with ML302F

All present enzymatic activity of Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with ML302F:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with ML302F, PDB code: 4tyt was solved by J.Brem, S.S.Van Berkel, M.A.Mcdonough, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.05 / 1.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 53.079, 61.358, 69.416, 90.00, 93.00, 90.00
R / Rfree (%) 15 / 20.1

Other elements in 4tyt:

The structure of Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with ML302F also contains other interesting chemical elements:

Chlorine (Cl) 6 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with ML302F (pdb code 4tyt). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with ML302F, PDB code: 4tyt:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4tyt

Go back to Zinc Binding Sites List in 4tyt
Zinc binding site 1 out of 2 in the Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with ML302F


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with ML302F within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:21.0
occ:1.00
OD1 A:ASP120 2.2 18.8 1.0
NE2 A:HIS240 2.2 17.7 1.0
SG A:CYS198 2.2 16.6 1.0
O8 A:S3C303 2.3 32.4 0.3
O8 A:S3C303 2.3 32.3 0.7
S9 A:S3C303 2.4 17.5 0.7
S9 A:S3C303 2.5 27.0 0.3
C6 A:S3C303 3.0 32.7 0.7
C6 A:S3C303 3.1 31.9 0.3
C5 A:S3C303 3.1 29.4 0.7
CG A:ASP120 3.1 25.1 1.0
CD2 A:HIS240 3.1 17.6 1.0
CE1 A:HIS240 3.2 17.2 1.0
C5 A:S3C303 3.2 30.5 0.3
CB A:CYS198 3.3 16.2 1.0
OD2 A:ASP120 3.5 18.8 1.0
ZN A:ZN302 3.8 15.5 1.0
NH2 A:ARG121 4.0 25.5 1.0
NE A:ARG121 4.1 17.8 1.0
O7 A:S3C303 4.2 31.7 0.7
CE1 A:HIS116 4.2 13.0 1.0
O7 A:S3C303 4.3 31.9 0.3
ND1 A:HIS240 4.3 18.9 1.0
CG A:HIS240 4.3 19.6 1.0
C4 A:S3C303 4.4 28.2 0.7
CB A:ASP120 4.4 21.2 1.0
NE2 A:HIS179 4.4 12.2 1.0
CZ A:ARG121 4.4 25.7 1.0
NE2 A:HIS116 4.4 11.9 1.0
C4 A:S3C303 4.5 29.7 0.3
CL2 A:S3C303 4.5 30.5 0.7
O A:HOH515 4.5 19.4 1.0
CA A:CYS198 4.6 15.4 1.0
CL1 A:S3C303 4.8 30.3 0.3
CE1 A:HIS179 4.9 15.3 1.0

Zinc binding site 2 out of 2 in 4tyt

Go back to Zinc Binding Sites List in 4tyt
Zinc binding site 2 out of 2 in the Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with ML302F


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with ML302F within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:15.5
occ:1.00
ND1 A:HIS118 2.0 14.6 1.0
NE2 A:HIS179 2.0 12.2 1.0
NE2 A:HIS116 2.1 11.9 1.0
S9 A:S3C303 2.3 17.5 0.7
S9 A:S3C303 2.3 27.0 0.3
CG A:HIS118 3.0 18.9 1.0
CD2 A:HIS179 3.0 11.1 1.0
CE1 A:HIS116 3.0 13.0 1.0
CE1 A:HIS118 3.0 17.8 1.0
CE1 A:HIS179 3.1 15.3 1.0
CD2 A:HIS116 3.1 14.4 1.0
C5 A:S3C303 3.1 29.4 0.7
C5 A:S3C303 3.2 30.5 0.3
CB A:HIS118 3.3 19.0 1.0
ZN A:ZN301 3.8 21.0 1.0
C6 A:S3C303 3.9 31.9 0.3
C6 A:S3C303 3.9 32.7 0.7
O8 A:S3C303 4.0 32.3 0.7
O8 A:S3C303 4.0 32.4 0.3
C4 A:S3C303 4.0 28.2 0.7
OD2 A:ASP120 4.0 18.8 1.0
C4 A:S3C303 4.1 29.7 0.3
ND1 A:HIS116 4.1 10.7 1.0
NE2 A:HIS118 4.1 15.4 1.0
CD2 A:HIS118 4.1 17.3 1.0
C3 A:S3C303 4.1 27.9 0.7
CG A:HIS179 4.1 11.8 1.0
ND1 A:HIS179 4.1 11.8 1.0
C3 A:S3C303 4.2 30.3 0.3
CG A:HIS116 4.2 10.6 1.0
CB A:CYS198 4.3 16.2 1.0
C2 A:S3C303 4.3 27.0 0.7
CG2 A:THR180 4.3 13.3 1.0
C10 A:S3C303 4.3 27.8 0.3
SG A:CYS198 4.4 16.6 1.0
CL2 A:S3C303 4.5 25.0 0.3
CL1 A:S3C303 4.5 26.3 0.7
C10 A:S3C303 4.7 32.4 0.7
CA A:HIS118 4.7 16.7 1.0
C2 A:S3C303 4.7 32.1 0.3
OD1 A:ASP120 4.8 18.8 1.0
CG A:ASP120 4.8 25.1 1.0
O7 A:S3C303 4.9 31.9 0.3
O7 A:S3C303 5.0 31.7 0.7

Reference:

J.Brem, S.S.Van Berkel, W.Aik, A.M.Rydzik, M.B.Avison, I.Pettinati, K.-D.Umland, A.Kawamura, J.Spencer, T.D.W.Claridge, M.A.Mcdonough, C.J.Schofield. Rhodanine Hydrolysis Leads to Potent Thioenolate Mediated Metallo-Beta-Lactamase Inhibition Nat.Chem. 2014.
ISSN: ESSN 1755-4349
DOI: 10.1038/NCHEM.2110
Page generated: Wed Dec 16 05:47:32 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy