Arsenic in PDB 6cx6: The Structure of An As(III) S-Adenosylmethionine Methyltransferase with As(III) and S-Adenosyl-L-Homocysteine (Sah)

All present enzymatic activity of The Structure of An As(III) S-Adenosylmethionine Methyltransferase with As(III) and S-Adenosyl-L-Homocysteine (Sah):
2.1.1.137;

The structure of The Structure of An As(III) S-Adenosylmethionine Methyltransferase with As(III) and S-Adenosyl-L-Homocysteine (Sah), PDB code: 6cx6 was solved by C.Packianathan, P.Kandavelu, B.P.Rosen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.87 / 2.84
Space group	P 42 2 2
Cell size a, b, c (Å), α, β, γ (°)	101.797, 101.797, 175.010, 90.00, 90.00, 90.00
R / Rfree (%)	21.5 / 29.1

The binding sites of Arsenic atom in the The Structure of An As(III) S-Adenosylmethionine Methyltransferase with As(III) and S-Adenosyl-L-Homocysteine (Sah) (pdb code 6cx6). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the The Structure of An As(III) S-Adenosylmethionine Methyltransferase with As(III) and S-Adenosyl-L-Homocysteine (Sah), PDB code: 6cx6:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in the The Structure of An As(III) S-Adenosylmethionine Methyltransferase with As(III) and S-Adenosyl-L-Homocysteine (Sah)


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of The Structure of An As(III) S-Adenosylmethionine Methyltransferase with As(III) and S-Adenosyl-L-Homocysteine (Sah) within 5.0Å range: probe atom residue distance (Å) B Occ A:As402 b:69.4 occ:1.00 SG A:CYS224 2.3 65.9 1.0 SG A:CYS174 2.3 65.4 1.0 SG A:CYS44 2.4 60.6 1.0 O A:CYS174 3.0 55.0 1.0 CB A:CYS224 3.1 70.2 1.0 CB A:CYS174 3.2 58.7 1.0 CB A:CYS44 3.6 55.9 1.0 C A:CYS174 3.9 49.3 1.0 O A:TYR70 4.0 70.6 1.0 CA A:CYS174 4.1 53.7 1.0 CA A:CYS44 4.3 60.9 1.0 CA A:CYS224 4.6 72.8 1.0 ND2 A:ASN177 4.8 62.1 1.0 SD A:SAH401 4.9 55.4 1.0 N A:CYS44 4.9 65.8 1.0

Arsenic binding site 2 out of 2 in the The Structure of An As(III) S-Adenosylmethionine Methyltransferase with As(III) and S-Adenosyl-L-Homocysteine (Sah)


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of The Structure of An As(III) S-Adenosylmethionine Methyltransferase with As(III) and S-Adenosyl-L-Homocysteine (Sah) within 5.0Å range: probe atom residue distance (Å) B Occ B:As402 b:60.2 occ:1.00 SG B:CYS224 2.0 44.9 1.0 SG B:CYS174 2.2 61.2 1.0 SG B:CYS44 2.6 54.0 1.0 O B:CYS174 3.0 67.7 1.0 CB B:CYS174 3.1 61.2 1.0 CB B:CYS224 3.2 50.1 1.0 CB B:CYS44 3.3 54.4 1.0 O B:TYR70 3.6 59.6 1.0 C B:CYS174 3.8 64.6 1.0 CA B:CYS174 3.9 63.9 1.0 CA B:CYS44 4.1 58.2 1.0 CA B:CYS224 4.6 52.0 1.0 ND2 B:ASN177 4.7 51.8 1.0 SD B:SAH401 4.7 56.3 1.0 C B:TYR70 4.8 60.5 1.0 N B:CYS44 4.8 58.8 1.0 O B:GLU223 4.8 58.5 1.0 CB B:TYR70 4.8 80.4 1.0 N B:CYS224 5.0 55.1 1.0

C.Packianathan, P.Kandavelu, B.P.Rosen. The Structure of An As(III) S-Adenosylmethionine Methyltransferase with 3-Coordinately Bound As(III) Depicts the First Step in Catalysis. Biochemistry V. 57 4083 2018.
ISSN: ISSN 1520-4995
PubMed: 29894638
DOI: 10.1021/ACS.BIOCHEM.8B00457