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Chlorine in PDB 1yxd: Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A

Enzymatic activity of Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A

All present enzymatic activity of Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A:
4.2.1.52;

Protein crystallography data

The structure of Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A, PDB code: 1yxd was solved by R.C.J.Dobson, M.D.W.Griffin, 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) 37.99 / 2.00
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 121.148, 121.148, 110.084, 90.00, 90.00, 120.00
R / Rfree (%) 15.9 / 18.6

Other elements in 1yxd:

The structure of Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A also contains other interesting chemical elements:

Potassium (K) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A (pdb code 1yxd). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A, PDB code: 1yxd:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1yxd

Go back to Chlorine Binding Sites List in 1yxd
Chlorine binding site 1 out of 2 in the Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1302

b:31.5
occ:1.00
NZ A:LYS161 2.9 16.9 1.0
O A:HOH1345 3.0 21.2 1.0
O A:HOH1349 3.1 21.8 1.0
CD2 A:LEU101 3.5 19.4 1.0
N A:THR44 3.5 20.8 1.0
CA A:GLY43 3.6 19.4 1.0
CG1 A:VAL40 3.9 20.5 1.0
C A:GLY43 4.0 19.9 1.0
CB A:ALA8 4.1 19.6 1.0
CG2 A:ILE203 4.2 18.3 1.0
CE2 A:TYR133 4.2 22.5 1.0
OG1 A:THR44 4.2 23.3 1.0
CE A:LYS161 4.2 18.7 1.0
OH A:TYR133 4.4 23.8 1.0
CB A:THR44 4.4 22.7 1.0
O A:HOH1535 4.5 40.1 1.0
CZ A:TYR133 4.5 21.3 1.0
CA A:THR44 4.5 21.6 1.0
CD A:LYS161 4.6 17.7 1.0
N A:GLY43 4.7 18.9 1.0
N A:THR45 4.7 20.1 1.0
CB A:VAL40 4.7 19.7 1.0
CA A:ALA8 4.8 20.0 1.0
CD2 A:TYR133 4.9 22.6 1.0
CG A:LEU101 4.9 19.1 1.0

Chlorine binding site 2 out of 2 in 1yxd

Go back to Chlorine Binding Sites List in 1yxd
Chlorine binding site 2 out of 2 in the Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl2302

b:27.4
occ:1.00
NZ B:LYS161 2.9 14.4 1.0
O B:HOH3360 2.9 21.5 1.0
O B:HOH3342 3.0 18.3 1.0
N B:THR44 3.6 18.3 1.0
CD2 B:LEU101 3.6 16.0 1.0
CA B:GLY43 3.8 18.2 1.0
CG1 B:VAL40 3.9 17.5 1.0
CB B:ALA8 4.0 15.2 1.0
C B:GLY43 4.1 17.7 1.0
CG2 B:ILE203 4.1 16.8 1.0
CE B:LYS161 4.2 13.4 1.0
CE2 B:TYR133 4.3 19.4 1.0
OG1 B:THR44 4.4 21.3 1.0
CB B:THR44 4.5 19.9 1.0
O B:HOH3501 4.5 36.5 1.0
OH B:TYR133 4.5 23.1 1.0
CA B:THR44 4.6 19.2 1.0
CD B:LYS161 4.6 13.4 1.0
CB B:VAL40 4.6 16.3 1.0
CA B:ALA8 4.7 15.5 1.0
CZ B:TYR133 4.7 17.9 1.0
N B:THR45 4.7 17.0 1.0
N B:GLY43 4.8 18.5 1.0

Reference:

R.C.Dobson, M.D.Griffin, G.B.Jameson, J.A.Gerrard. The Crystal Structures of Native and (S)-Lysine-Bound Dihydrodipicolinate Synthase From Escherichia Coli with Improved Resolution Show New Features of Biological Significance. Acta Crystallogr.,Sect.D V. 61 1116 2005.
ISSN: ISSN 0907-4449
PubMed: 16041077
DOI: 10.1107/S0907444905016318
Page generated: Sat Dec 12 08:56:29 2020

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