Cobalt in PDB 6vs5: Mycobacterium Tuberculosis Dihydrofolate Reductase in Complex with 5- Methyl-1-Phenyl-1H-Pyrazole-4-Carboxylic Acid (Fragment 1)

All present enzymatic activity of Mycobacterium Tuberculosis Dihydrofolate Reductase in Complex with 5- Methyl-1-Phenyl-1H-Pyrazole-4-Carboxylic Acid (Fragment 1):
1.5.1.3;

The structure of Mycobacterium Tuberculosis Dihydrofolate Reductase in Complex with 5- Methyl-1-Phenyl-1H-Pyrazole-4-Carboxylic Acid (Fragment 1), PDB code: 6vs5 was solved by J.A.Ribeiro, P.Tyrakis, T.Blundell, M.V.B.Dias, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.23 / 1.76
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.477, 70.453, 71.876, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 25.6

The binding sites of Cobalt atom in the Mycobacterium Tuberculosis Dihydrofolate Reductase in Complex with 5- Methyl-1-Phenyl-1H-Pyrazole-4-Carboxylic Acid (Fragment 1) (pdb code 6vs5). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Mycobacterium Tuberculosis Dihydrofolate Reductase in Complex with 5- Methyl-1-Phenyl-1H-Pyrazole-4-Carboxylic Acid (Fragment 1), PDB code: 6vs5:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Mycobacterium Tuberculosis Dihydrofolate Reductase in Complex with 5- Methyl-1-Phenyl-1H-Pyrazole-4-Carboxylic Acid (Fragment 1)


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Mycobacterium Tuberculosis Dihydrofolate Reductase in Complex with 5- Methyl-1-Phenyl-1H-Pyrazole-4-Carboxylic Acid (Fragment 1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Co201 b:21.2 occ:1.00 O A:HOH350 1.8 24.5 1.0 O A:HOH311 2.0 19.2 1.0 NE2 A:HIS38 2.1 17.3 1.0 NE2 B:HIS157 2.1 22.4 1.0 O A:HOH384 2.1 26.0 1.0 O A:HOH320 2.3 16.6 1.0 CE1 B:HIS157 3.0 17.7 1.0 CE1 A:HIS38 3.0 21.5 1.0 CD2 A:HIS38 3.1 17.9 1.0 CD2 B:HIS157 3.1 22.6 1.0 OE1 A:GLU90 3.8 24.8 1.0 O A:ILE34 3.8 15.8 1.0 O B:HOH330 4.1 31.5 1.0 OG1 B:THR108 4.1 22.8 1.0 O A:MET36 4.1 20.1 1.0 ND1 B:HIS157 4.2 21.4 1.0 OXT B:SER159 4.2 62.0 1.0 ND1 A:HIS38 4.2 20.7 1.0 OE2 A:GLU90 4.2 26.8 1.0 CG B:HIS157 4.2 21.6 1.0 CG A:HIS38 4.2 19.9 1.0 CD A:GLU90 4.3 26.2 1.0 O A:GLU33 4.4 18.3 1.0 O B:ARG158 4.5 31.2 1.0 C A:ILE34 4.6 19.9 1.0 O A:HOH336 4.7 23.1 1.0 C B:SER159 4.9 58.1 1.0

Cobalt binding site 2 out of 2 in the Mycobacterium Tuberculosis Dihydrofolate Reductase in Complex with 5- Methyl-1-Phenyl-1H-Pyrazole-4-Carboxylic Acid (Fragment 1)


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Mycobacterium Tuberculosis Dihydrofolate Reductase in Complex with 5- Methyl-1-Phenyl-1H-Pyrazole-4-Carboxylic Acid (Fragment 1) within 5.0Å range: probe atom residue distance (Å) B Occ B:Co201 b:26.9 occ:1.00 O B:HOH333 1.9 26.8 1.0 O B:HOH350 1.9 33.5 1.0 NE2 B:HIS38 2.1 20.8 1.0 O B:HOH368 2.2 25.7 1.0 O B:HOH324 2.3 17.5 1.0 NE2 A:HIS157 2.9 43.9 1.0 CE1 B:HIS38 3.1 16.0 1.0 CD2 B:HIS38 3.1 17.3 1.0 CE1 A:HIS157 3.3 42.0 1.0 O B:ILE34 3.7 17.4 1.0 OE1 B:GLU90 3.8 27.2 1.0 O B:HOH348 3.8 24.3 1.0 OE2 B:GLU90 4.2 27.1 1.0 ND1 B:HIS38 4.2 16.0 1.0 CD2 A:HIS157 4.2 40.1 1.0 CG B:HIS38 4.2 17.9 1.0 CD B:GLU90 4.3 28.8 1.0 O B:MET36 4.3 21.0 1.0 O A:HOH417 4.3 36.1 1.0 O A:ARG158 4.4 33.1 1.0 O B:HOH386 4.5 29.7 1.0 O B:GLU33 4.5 24.9 1.0 CB A:THR108 4.6 23.1 1.0 ND1 A:HIS157 4.6 40.0 1.0 OG1 A:THR108 4.6 23.2 1.0 C B:ILE34 4.6 15.9 1.0 CA A:SER159 4.7 40.6 1.0 CG2 A:THR108 4.7 17.2 1.0

J.A.Ribeiro, A.Hammer, G.A.Libreros-Zuniga, S.M.Chavez-Pacheco, P.Tyrakis, G.S.De Oliveira, T.Kirkman, J.El Bakali, S.A.Rocco, M.L.Sforca, R.Parise-Filho, A.G.Coyne, T.L.Blundell, C.Abell, M.V.B.Dias. Using A Fragment-Based Approach to Identify Alternative Chemical Scaffolds Targeting Dihydrofolate Reductase Frommycobacterium Tuberculosis. Acs Infect Dis. V. 6 2192 2020.
ISSN: ESSN 2373-8227
PubMed: 32603583
DOI: 10.1021/ACSINFECDIS.0C00263