Atomistry » Chlorine » PDB 4g81-4gen » 4gci
Atomistry »
  Chlorine »
    PDB 4g81-4gen »
      4gci »

Chlorine in PDB 4gci: Crystal Structure of Glutahtione S-Transferase Homolog From Yersinia Pestis, Target Efi-501894, with Bound Glutathione, Monoclinic Form

Protein crystallography data

The structure of Crystal Structure of Glutahtione S-Transferase Homolog From Yersinia Pestis, Target Efi-501894, with Bound Glutathione, Monoclinic Form, PDB code: 4gci was solved by M.W.Vetting, R.Toro, R.Bhosle, N.F.Al Obaidi, L.L.Morisco, S.R.Wasserman, S.Sojitra, E.Washington, A.Scott Glenn, S.Chowdhury, B.Evans, J.Hammonds, B.Hillerich, J.Love, R.D.Seidel, H.J.Imker, R.N.Armstrong, J.A.Gerlt, S.C.Almo, Enzyme Function Initiative (Efi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.87 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 48.741, 89.338, 57.546, 90.00, 112.26, 90.00
R / Rfree (%) 17.6 / 20.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Glutahtione S-Transferase Homolog From Yersinia Pestis, Target Efi-501894, with Bound Glutathione, Monoclinic Form (pdb code 4gci). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Glutahtione S-Transferase Homolog From Yersinia Pestis, Target Efi-501894, with Bound Glutathione, Monoclinic Form, PDB code: 4gci:

Chlorine binding site 1 out of 1 in 4gci

Go back to Chlorine Binding Sites List in 4gci
Chlorine binding site 1 out of 1 in the Crystal Structure of Glutahtione S-Transferase Homolog From Yersinia Pestis, Target Efi-501894, with Bound Glutathione, Monoclinic Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Glutahtione S-Transferase Homolog From Yersinia Pestis, Target Efi-501894, with Bound Glutathione, Monoclinic Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:79.2
occ:1.00
O A:HOH623 2.7 58.1 1.0
N A:PHE26 3.2 33.5 1.0
O A:PHE26 3.3 34.4 1.0
CA A:ASP25 3.6 40.4 1.0
OD1 A:ASP25 3.8 54.3 1.0
C A:ASP25 3.9 31.8 1.0
O A:LEU24 4.1 37.5 1.0
C A:PHE26 4.2 30.2 1.0
CB A:ASP25 4.2 41.7 1.0
CD1 A:PHE26 4.3 30.5 1.0
CA A:PHE26 4.3 28.3 1.0
CG A:ASP25 4.4 53.2 1.0
CE1 A:PHE26 4.6 28.1 1.0
N A:ASP25 4.6 36.7 1.0
O A:HOH513 4.7 44.7 0.5
CG A:PHE26 4.8 31.3 1.0
C A:LEU24 4.8 32.7 1.0
SD A:MET1 4.8 48.0 1.0
O A:HOH513 5.0 35.1 0.5

Reference:

M.W.Vetting, R.Toro, R.Bhosle, N.F.Al Obaidi, L.L.Morisco, S.R.Wasserman, S.Sojitra, E.Washington, A.Scott Glenn, S.Chowdhury, B.Evans, J.Hammonds, B.Hillerich, J.Love, R.D.Seidel, H.J.Imker, R.N.Armstrong, J.A.Gerlt, S.C.Almo, Enzyme Function Initiative (Efi). Crystal Structure of Glutahtione S-Transferase Homolog From Yersinia Pestis, Target Efi-501894, with Bound Glutathione, Monoclinic Form To Be Published.
Page generated: Sun Jul 21 14:29:41 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