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 / R_free (%)*	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

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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

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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

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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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