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Potassium in PDB 6oxd: Structure of Mycobacterium Tuberculosis Methylmalonyl-Coa Mutase with Adenosyl Cobalamin

Enzymatic activity of Structure of Mycobacterium Tuberculosis Methylmalonyl-Coa Mutase with Adenosyl Cobalamin

All present enzymatic activity of Structure of Mycobacterium Tuberculosis Methylmalonyl-Coa Mutase with Adenosyl Cobalamin:
5.4.99.2;

Protein crystallography data

The structure of Structure of Mycobacterium Tuberculosis Methylmalonyl-Coa Mutase with Adenosyl Cobalamin, PDB code: 6oxd was solved by M.Purchal, M.Ruetz, R.Banerjee, M.Koutmos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.80 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 76.576, 104.957, 194.088, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / 19.7

Other elements in 6oxd:

The structure of Structure of Mycobacterium Tuberculosis Methylmalonyl-Coa Mutase with Adenosyl Cobalamin also contains other interesting chemical elements:

Cobalt (Co) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of Mycobacterium Tuberculosis Methylmalonyl-Coa Mutase with Adenosyl Cobalamin (pdb code 6oxd). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Structure of Mycobacterium Tuberculosis Methylmalonyl-Coa Mutase with Adenosyl Cobalamin, PDB code: 6oxd:

Potassium binding site 1 out of 1 in 6oxd

Go back to Potassium Binding Sites List in 6oxd
Potassium binding site 1 out of 1 in the Structure of Mycobacterium Tuberculosis Methylmalonyl-Coa Mutase with Adenosyl Cobalamin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Mycobacterium Tuberculosis Methylmalonyl-Coa Mutase with Adenosyl Cobalamin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1003

b:26.8
occ:1.00
OD1 A:ASP160 2.7 24.2 1.0
O A:HOH1175 2.7 25.9 1.0
O A:TYR141 2.7 29.1 1.0
O A:ILE159 2.7 25.3 1.0
OG1 A:THR137 3.0 28.6 1.0
HA A:THR137 3.1 31.3 1.0
HA A:ASP142 3.2 39.5 1.0
H A:ILE159 3.6 31.7 1.0
C A:ILE159 3.6 23.0 1.0
HA A:ASP160 3.6 36.0 1.0
CA A:THR137 3.7 26.1 1.0
N A:THR137 3.7 23.2 1.0
CG A:ASP160 3.7 27.7 1.0
HG A:SER143 3.7 32.2 1.0
H A:SER143 3.8 32.9 1.0
H A:THR137 3.8 27.8 1.0
HB3 A:ALA136 3.8 35.5 1.0
CB A:THR137 3.8 27.4 1.0
C A:TYR141 3.9 26.4 1.0
HG23 A:THR137 3.9 30.8 1.0
CA A:ASP142 4.0 32.9 1.0
N A:SER143 4.0 27.4 1.0
HB1 A:ALA136 4.1 35.5 1.0
N A:ILE159 4.1 26.4 1.0
HB A:VAL564 4.2 36.8 1.0
C A:ASP142 4.2 28.0 1.0
C A:ALA136 4.2 26.7 1.0
HG11 A:VAL564 4.2 34.0 1.0
N A:ASP160 4.2 24.1 1.0
OG A:SER143 4.3 26.8 1.0
CA A:ASP160 4.3 30.0 1.0
OD1 A:ASP134 4.3 24.0 1.0
CB A:ALA136 4.4 29.6 1.0
N A:ASP142 4.4 29.4 1.0
CG2 A:THR137 4.4 25.6 1.0
OD2 A:ASP160 4.5 28.4 1.0
CA A:ILE159 4.5 29.3 1.0
HA A:SER143 4.5 40.0 1.0
HG21 A:VAL564 4.6 35.7 1.0
CB A:ASP160 4.6 24.5 1.0
HA A:ALA158 4.6 28.0 1.0
O A:ALA136 4.6 25.2 1.0
HB A:THR137 4.7 32.9 1.0
HB1 A:ALA158 4.7 31.7 1.0
CA A:SER143 4.8 33.3 1.0
H A:TYR141 4.8 32.2 1.0
HG21 A:THR137 4.9 30.8 1.0
CG1 A:VAL564 4.9 28.4 1.0
OD2 A:ASP134 4.9 25.2 1.0
CB A:VAL564 4.9 30.7 1.0
HB A:ILE159 4.9 32.9 1.0
CA A:ALA136 4.9 25.1 1.0
H A:ASP160 4.9 28.9 1.0
HG12 A:VAL564 5.0 34.0 1.0
OD1 A:ASP142 5.0 34.9 1.0

Reference:

M.Ruetz, G.C.Campanello, M.Purchal, H.Shen, L.Mcdevitt, H.Gouda, S.Wakabayashi, J.Zhu, E.J.Rubin, K.Warncke, V.K.Mootha, M.Koutmos, R.Banerjee. Itaconyl-Coa Forms A Stable Biradical in Methylmalonyl-Coa Mutase and Derails Its Activity and Repair. Science V. 366 589 2019.
ISSN: ESSN 1095-9203
PubMed: 31672889
DOI: 10.1126/SCIENCE.AAY0934
Page generated: Mon Dec 14 01:03:32 2020

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