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Chlorine in PDB 9cya: C387S Variant of D-Ornithine/D-Lysine Decarboxylase Complexed with Hepes and Putrescine

Enzymatic activity of C387S Variant of D-Ornithine/D-Lysine Decarboxylase Complexed with Hepes and Putrescine

All present enzymatic activity of C387S Variant of D-Ornithine/D-Lysine Decarboxylase Complexed with Hepes and Putrescine:
4.1.1.116;

Protein crystallography data

The structure of C387S Variant of D-Ornithine/D-Lysine Decarboxylase Complexed with Hepes and Putrescine, PDB code: 9cya was solved by R.S.Phillips, S.Blankenship, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 59.82 / 1.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 139.387, 50.591, 73.308, 90, 120.88, 90
R / Rfree (%) 15.3 / 18.2

Other elements in 9cya:

The structure of C387S Variant of D-Ornithine/D-Lysine Decarboxylase Complexed with Hepes and Putrescine also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the C387S Variant of D-Ornithine/D-Lysine Decarboxylase Complexed with Hepes and Putrescine (pdb code 9cya). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the C387S Variant of D-Ornithine/D-Lysine Decarboxylase Complexed with Hepes and Putrescine, PDB code: 9cya:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 9cya

Go back to Chlorine Binding Sites List in 9cya
Chlorine binding site 1 out of 2 in the C387S Variant of D-Ornithine/D-Lysine Decarboxylase Complexed with Hepes and Putrescine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of C387S Variant of D-Ornithine/D-Lysine Decarboxylase Complexed with Hepes and Putrescine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl501

b:23.5
occ:1.00
H A:THR75 2.4 19.6 1.0
HG A:CYS97 2.8 22.4 1.0
HA A:LYS74 3.1 19.5 1.0
HA A:ILE96 3.1 18.4 1.0
O A:HOH727 3.2 27.4 1.0
N A:THR75 3.3 16.3 1.0
HG3 A:LYS74 3.3 29.1 1.0
O A:HOH746 3.4 29.8 1.0
O A:HOH951 3.5 39.0 1.0
HB A:THR75 3.5 18.8 1.0
HG22 A:ILE96 3.7 20.6 1.0
O A:THR75 3.8 16.6 1.0
H A:CYS97 3.9 19.6 1.0
CA A:LYS74 3.9 16.2 1.0
HB A:ILE96 4.0 19.2 1.0
CA A:ILE96 4.0 15.3 1.0
SG A:CYS97 4.0 18.7 1.0
O A:GLY95 4.1 19.7 1.0
C A:LYS74 4.1 17.0 1.0
CG A:LYS74 4.1 24.3 1.0
HE21 A:GLN64 4.1 33.0 1.0
HE22 A:GLN64 4.1 33.0 1.0
HG1 A:THR75 4.1 22.5 1.0
CA A:THR75 4.1 15.6 1.0
CB A:THR75 4.2 15.7 1.0
HG2 A:LYS74 4.2 29.1 1.0
N A:CYS97 4.3 16.3 1.0
CB A:ILE96 4.3 16.0 1.0
CG2 A:ILE96 4.3 17.2 1.0
C A:THR75 4.4 15.8 1.0
NE2 A:GLN64 4.4 27.5 1.0
HG21 A:ILE96 4.5 20.6 1.0
O A:THR73 4.5 19.5 0.7
HB2 A:CYS97 4.5 18.4 1.0
C A:ILE96 4.5 16.8 1.0
CB A:LYS74 4.6 19.8 1.0
OG1 A:THR75 4.6 18.8 1.0
O A:THR73 4.7 21.1 0.3
CB A:CYS97 4.8 15.3 1.0
HE3 A:LYS74 4.9 34.0 1.0
C A:GLY95 5.0 17.9 1.0
N A:ILE96 5.0 15.9 1.0

Chlorine binding site 2 out of 2 in 9cya

Go back to Chlorine Binding Sites List in 9cya
Chlorine binding site 2 out of 2 in the C387S Variant of D-Ornithine/D-Lysine Decarboxylase Complexed with Hepes and Putrescine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of C387S Variant of D-Ornithine/D-Lysine Decarboxylase Complexed with Hepes and Putrescine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl512

b:33.3
occ:1.00
O A:HOH1009 2.8 47.6 1.0
O A:HOH923 2.9 21.7 1.0
HE22 A:GLN196 2.9 44.1 1.0
HD12 A:LEU147 3.5 34.8 1.0
NE2 A:GLN196 3.7 36.8 1.0
HE21 A:GLN196 3.9 44.1 1.0
O A:HOH695 4.0 28.6 1.0
HB2 A:LEU147 4.1 25.3 1.0
CD1 A:LEU147 4.4 29.0 1.0
HG A:LEU147 4.4 34.6 1.0
H A:LEU147 4.6 23.3 1.0
O A:HOH997 4.6 28.5 1.0
HD11 A:LEU147 4.7 34.8 1.0
CD A:GLN196 4.8 32.8 1.0
CG A:LEU147 4.8 28.8 1.0
CB A:LEU147 4.9 21.1 1.0

Reference:

R.S.Phillips, S.Blankenship. Structure of C387S Variant of D-Ornithine/D-Lysine Decarboxylase Complexed with Hepes and Putrescine To Be Published.
Page generated: Sat Aug 23 00:39:24 2025

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