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Chlorine in PDB 2ats: Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine

Enzymatic activity of Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine

All present enzymatic activity of Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine:
4.2.1.52;

Protein crystallography data

The structure of Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine, PDB code: 2ats was solved by S.R.A.Devenish, R.C.J.Dobson, G.B.Jameson, J.A.Gerrard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.80 / 1.90
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 121.680, 121.680, 109.799, 90.00, 90.00, 120.00
R / Rfree (%) 16.8 / 20.2

Other elements in 2ats:

The structure of Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine also contains other interesting chemical elements:

Potassium (K) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine (pdb code 2ats). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine, PDB code: 2ats:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 2ats

Go back to Chlorine Binding Sites List in 2ats
Chlorine binding site 1 out of 2 in the Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2001

b:24.2
occ:1.00
NZ A:LYS161 3.0 13.9 1.0
O A:HOH3027 3.0 16.4 1.0
O A:HOH3047 3.1 19.1 1.0
CD2 A:LEU101 3.5 16.9 1.0
N A:THR44 3.6 17.8 1.0
CA A:GLY43 3.7 17.4 1.0
CG1 A:VAL40 3.8 17.4 1.0
CB A:ALA8 4.0 18.2 1.0
CG2 A:ILE203 4.0 14.9 1.0
C A:GLY43 4.1 17.2 1.0
CE2 A:TYR133 4.2 18.9 1.0
CE A:LYS161 4.3 16.4 1.0
OG1 A:THR44 4.3 17.1 1.0
OH A:TYR133 4.4 21.1 1.0
CB A:THR44 4.4 18.6 1.0
O A:HOH3301 4.4 50.0 1.0
CZ A:TYR133 4.6 18.6 1.0
CD A:LYS161 4.6 17.5 1.0
CA A:THR44 4.6 17.6 1.0
CB A:VAL40 4.7 16.4 1.0
CA A:ALA8 4.7 18.3 1.0
N A:GLY43 4.8 17.2 1.0
N A:THR45 4.8 17.3 1.0
CG A:LEU101 5.0 17.5 1.0
CD2 A:TYR133 5.0 18.5 1.0

Chlorine binding site 2 out of 2 in 2ats

Go back to Chlorine Binding Sites List in 2ats
Chlorine binding site 2 out of 2 in the Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl2002

b:22.5
occ:1.00
NZ B:LYS161 3.0 10.4 1.0
O B:HOH2025 3.0 14.8 1.0
O B:HOH2034 3.1 16.7 1.0
CD2 B:LEU101 3.5 17.5 1.0
N B:THR44 3.5 17.5 1.0
CA B:GLY43 3.7 16.9 1.0
CG1 B:VAL40 3.8 14.4 1.0
CB B:ALA8 4.0 15.1 1.0
CG2 B:ILE203 4.1 15.8 1.0
C B:GLY43 4.1 17.2 1.0
CE B:LYS161 4.2 10.9 1.0
OG1 B:THR44 4.3 19.3 1.0
CE2 B:TYR133 4.3 16.7 1.0
CB B:THR44 4.4 18.9 1.0
OH B:TYR133 4.4 16.8 1.0
CA B:THR44 4.5 18.2 1.0
CB B:VAL40 4.6 14.5 1.0
O B:HOH2254 4.6 38.6 1.0
CD B:LYS161 4.6 13.2 1.0
CZ B:TYR133 4.7 15.1 1.0
CA B:ALA8 4.7 14.6 1.0
N B:THR45 4.7 16.5 1.0
N B:GLY43 4.8 17.0 1.0
CG B:LEU101 4.9 15.7 1.0

Reference:

S.R.A.Devenish, R.C.J.Dobson, G.B.Jameson, J.A.Gerrard. The Co-Crystallisation of (S)-Lysine-Bound Dihydrodipicolinate Synthase From E. Coli Indicates That Domain Movements Are Not Responsible For (S)-Lysine Inhibition To Be Published.
Page generated: Sat Dec 12 08:59:13 2020

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