Atomistry » Chlorine » PDB 4kwt-4lb4 » 4kzf
Atomistry »
  Chlorine »
    PDB 4kwt-4lb4 »
      4kzf »

Chlorine in PDB 4kzf: The Mechanism of the Amidases: the Effect of the Mutation E142L in the Amidase From Geobacillus Pallidus

Enzymatic activity of The Mechanism of the Amidases: the Effect of the Mutation E142L in the Amidase From Geobacillus Pallidus

All present enzymatic activity of The Mechanism of the Amidases: the Effect of the Mutation E142L in the Amidase From Geobacillus Pallidus:
3.5.1.4;

Protein crystallography data

The structure of The Mechanism of the Amidases: the Effect of the Mutation E142L in the Amidase From Geobacillus Pallidus, PDB code: 4kzf was solved by B.W.Weber, B.T.Sewell, S.W.Kimani, A.Varsani, D.A.Cowan, R.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.30 / 1.85
Space group P 42 3 2
Cell size a, b, c (Å), α, β, γ (°) 130.979, 130.979, 130.979, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 20.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Mechanism of the Amidases: the Effect of the Mutation E142L in the Amidase From Geobacillus Pallidus (pdb code 4kzf). 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 The Mechanism of the Amidases: the Effect of the Mutation E142L in the Amidase From Geobacillus Pallidus, PDB code: 4kzf:

Chlorine binding site 1 out of 1 in 4kzf

Go back to Chlorine Binding Sites List in 4kzf
Chlorine binding site 1 out of 1 in the The Mechanism of the Amidases: the Effect of the Mutation E142L in the Amidase From Geobacillus Pallidus


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Mechanism of the Amidases: the Effect of the Mutation E142L in the Amidase From Geobacillus Pallidus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl401

b:35.4
occ:1.00
 N A:TRP138 2.9 26.7 1.0
NZ A:LYS134 3.0 32.0 1.0
CD1 A:TRP144 3.3 25.1 1.0
CB A:LEU142 3.5 38.4 1.0
OH A:TYR60 3.5 24.6 1.0
CA A:PRO137 3.7 26.4 1.0
CB A:TRP138 3.7 25.4 1.0
CE A:LYS134 3.8 27.4 1.0
C A:PRO137 3.8 27.2 1.0
CA A:TRP138 3.8 25.1 1.0
CD A:LYS134 3.9 27.2 1.0
NE1 A:TRP144 3.9 26.7 1.0
CB A:PRO137 4.0 29.0 1.0
ND2 A:ASN117 4.1 21.1 1.0
CG A:LEU142 4.2 45.3 1.0
OE2 A:GLU59 4.4 16.3 1.0
C A:TRP138 4.5 27.0 1.0
CG A:TRP144 4.6 25.6 1.0
O A:TRP138 4.8 29.1 1.0
CZ A:TYR60 4.8 24.4 1.0
CA A:LEU142 4.9 37.1 1.0
O A:LEU142 4.9 32.4 1.0
O A:PRO137 5.0 27.0 1.0
C A:LEU142 5.0 37.1 1.0

Reference:

B.W.Weber, S.W.Kimani, A.Varsani, D.A.Cowan, R.Hunter, G.A.Venter, J.C.Gumbart, B.T.Sewell. The Mechanism of the Amidases: Mutating the Glutamate Adjacent to the Catalytic Triad Inactivates the Enzyme Due to Substrate Mispositioning. J.Biol.Chem. V. 288 28514 2013.
ISSN: ISSN 0021-9258
PubMed: 23946488
DOI: 10.1074/JBC.M113.503284
Page generated: Sun Jul 21 18:38:50 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