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Chlorine in PDB 5tek: Apo Structure of 4-Hydroxy-Tetrahydrodipicolinate Reductase From Mycobacterium Tuberculosis

Enzymatic activity of Apo Structure of 4-Hydroxy-Tetrahydrodipicolinate Reductase From Mycobacterium Tuberculosis

All present enzymatic activity of Apo Structure of 4-Hydroxy-Tetrahydrodipicolinate Reductase From Mycobacterium Tuberculosis:
1.17.1.8;

Protein crystallography data

The structure of Apo Structure of 4-Hydroxy-Tetrahydrodipicolinate Reductase From Mycobacterium Tuberculosis, PDB code: 5tek was solved by N.Mank, S.Pote, K.Arnette, V.Klapper, M.Chruszcz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.01
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 60.569, 122.607, 80.846, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 21.7

Other elements in 5tek:

The structure of Apo Structure of 4-Hydroxy-Tetrahydrodipicolinate Reductase From Mycobacterium Tuberculosis also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Apo Structure of 4-Hydroxy-Tetrahydrodipicolinate Reductase From Mycobacterium Tuberculosis (pdb code 5tek). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Apo Structure of 4-Hydroxy-Tetrahydrodipicolinate Reductase From Mycobacterium Tuberculosis, PDB code: 5tek:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 5tek

Go back to Chlorine Binding Sites List in 5tek
Chlorine binding site 1 out of 3 in the Apo Structure of 4-Hydroxy-Tetrahydrodipicolinate Reductase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Apo Structure of 4-Hydroxy-Tetrahydrodipicolinate Reductase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:89.4
occ:1.00
 N A:GLY143 3.4 64.4 1.0
N A:THR144 3.7 61.3 1.0
CB A:SER142 3.7 61.8 1.0
NZ A:LYS137 3.7 74.0 1.0
CA A:GLY143 3.9 65.4 1.0
OG1 A:THR144 3.9 62.8 1.0
C A:SER142 4.3 63.4 1.0
C A:GLY143 4.3 63.0 1.0
CA A:SER142 4.3 62.2 1.0
OG A:SER142 4.4 59.7 1.0
CB A:THR144 4.5 59.0 1.0
CE A:LYS137 4.5 71.8 1.0
CA A:THR144 4.7 58.8 1.0
OD2 A:ASP139 4.9 91.8 1.0

Chlorine binding site 2 out of 3 in 5tek

Go back to Chlorine Binding Sites List in 5tek
Chlorine binding site 2 out of 3 in the Apo Structure of 4-Hydroxy-Tetrahydrodipicolinate Reductase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Apo Structure of 4-Hydroxy-Tetrahydrodipicolinate Reductase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl301

b:74.2
occ:1.00
 N B:GLY143 3.7 54.8 1.0
N B:THR144 3.7 50.2 1.0
OG1 B:THR144 3.8 49.2 1.0
NZ B:LYS137 3.9 60.7 1.0
CB B:SER142 4.0 52.2 1.0
CA B:GLY143 4.1 54.4 1.0
C B:GLY143 4.4 53.5 1.0
CB B:THR144 4.5 46.1 1.0
C B:SER142 4.5 52.9 1.0
OG B:SER142 4.6 51.1 1.0
CA B:SER142 4.6 53.6 1.0
CA B:THR144 4.7 47.9 1.0
CE B:LYS137 4.7 59.3 1.0

Chlorine binding site 3 out of 3 in 5tek

Go back to Chlorine Binding Sites List in 5tek
Chlorine binding site 3 out of 3 in the Apo Structure of 4-Hydroxy-Tetrahydrodipicolinate Reductase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Apo Structure of 4-Hydroxy-Tetrahydrodipicolinate Reductase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl302

b:86.7
occ:1.00
 O B:HOH491 3.2 71.0 1.0
NE2 B:HIS134 3.5 54.7 1.0
NZ B:LYS137 3.7 60.7 1.0
CE1 B:HIS134 3.9 56.2 1.0
CG B:LYS137 4.1 60.0 1.0
CD B:LYS137 4.2 58.5 1.0
CB B:LYS137 4.4 59.7 1.0
CE B:LYS137 4.6 59.3 1.0
CA B:LYS137 4.7 59.7 1.0
CD2 B:HIS134 4.7 54.2 1.0

Reference:

M.Chruszcz, N.Mank, S.Pote, K.Arnette, V.Klapper, M.Chruszcz. N/A N/A.
Page generated: Fri Jul 26 17:25:58 2024

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