Iron in PDB 4m6x: Mutant Structure of Methyltransferase From Streptomyces Hygroscopicus Complexed with S-Adenosyl-L-Homocysteine and Methylphenylpyruvic Acid

The structure of Mutant Structure of Methyltransferase From Streptomyces Hygroscopicus Complexed with S-Adenosyl-L-Homocysteine and Methylphenylpyruvic Acid, PDB code: 4m6x was solved by Y.C.Liu, X.W.Zou, H.C.Chan, C.J.Huang, T.L.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.94 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.009, 90.219, 136.505, 90.00, 90.00, 90.00
R / Rfree (%)	16.2 / 22.7

The structure of Mutant Structure of Methyltransferase From Streptomyces Hygroscopicus Complexed with S-Adenosyl-L-Homocysteine and Methylphenylpyruvic Acid also contains other interesting chemical elements:

Calcium

(Ca)

5 atoms

The binding sites of Iron atom in the Mutant Structure of Methyltransferase From Streptomyces Hygroscopicus Complexed with S-Adenosyl-L-Homocysteine and Methylphenylpyruvic Acid (pdb code 4m6x). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Mutant Structure of Methyltransferase From Streptomyces Hygroscopicus Complexed with S-Adenosyl-L-Homocysteine and Methylphenylpyruvic Acid, PDB code: 4m6x:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Mutant Structure of Methyltransferase From Streptomyces Hygroscopicus Complexed with S-Adenosyl-L-Homocysteine and Methylphenylpyruvic Acid


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Mutant Structure of Methyltransferase From Streptomyces Hygroscopicus Complexed with S-Adenosyl-L-Homocysteine and Methylphenylpyruvic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe403 b:32.0 occ:1.00 O A:HOH501 2.0 26.9 1.0 OAK A:56D402 2.1 51.6 1.0 NE2 A:HIS243 2.2 33.8 1.0 NE2 A:HIS295 2.3 27.1 1.0 O A:HOH502 2.4 34.8 1.0 OAL A:56D402 2.5 66.8 1.0 CAH A:56D402 2.9 60.4 1.0 CE1 A:HIS243 3.0 29.8 1.0 CAI A:56D402 3.1 61.0 1.0 CE1 A:HIS295 3.2 27.8 1.0 CD2 A:HIS295 3.3 27.2 1.0 CD2 A:HIS243 3.4 32.8 1.0 ND1 A:HIS243 4.2 31.9 1.0 OAM A:56D402 4.3 56.2 1.0 OE1 A:GLU244 4.3 58.7 1.0 ND1 A:HIS295 4.3 28.2 1.0 CAG A:56D402 4.4 60.8 1.0 CG A:HIS295 4.4 27.2 1.0 CG A:HIS243 4.4 32.5 1.0 OE2 A:GLU244 4.6 59.9 1.0 CD A:GLU244 4.8 54.3 1.0 CAE A:56D402 4.8 57.3 1.0 CE1 A:PHE291 4.9 31.4 1.0 CAJ A:56D402 5.0 60.6 1.0

Iron binding site 2 out of 2 in the Mutant Structure of Methyltransferase From Streptomyces Hygroscopicus Complexed with S-Adenosyl-L-Homocysteine and Methylphenylpyruvic Acid


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Mutant Structure of Methyltransferase From Streptomyces Hygroscopicus Complexed with S-Adenosyl-L-Homocysteine and Methylphenylpyruvic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe403 b:28.1 occ:1.00 OAK B:56D402 1.9 34.0 1.0 O B:HOH721 2.2 37.6 1.0 NE2 B:HIS295 2.2 24.8 1.0 OAM B:56D402 2.2 47.4 1.0 NE2 B:HIS243 2.3 27.0 1.0 O B:HOH501 2.3 29.0 1.0 CAH B:56D402 2.6 42.9 1.0 CAI B:56D402 2.7 44.0 1.0 CE1 B:HIS243 3.1 25.7 1.0 CE1 B:HIS295 3.1 24.2 1.0 CD2 B:HIS295 3.3 25.8 1.0 CD2 B:HIS243 3.4 26.5 1.0 OAL B:56D402 4.0 41.8 1.0 CAG B:56D402 4.1 46.2 1.0 ND1 B:HIS295 4.2 26.4 1.0 ND1 B:HIS243 4.3 25.4 1.0 CG B:HIS295 4.4 25.3 1.0 OE2 B:GLU244 4.4 46.4 1.0 CG B:HIS243 4.4 25.6 1.0 CAJ B:56D402 4.6 44.7 1.0 CAE B:56D402 4.7 46.4 1.0 CAD B:56D402 4.8 47.8 1.0 CE1 B:PHE291 4.9 29.7 1.0

X.W.Zou, Y.C.Liu, N.S.Hsu, C.J.Huang, S.Y.Lyu, H.C.Chan, C.Y.Chang, H.W.Yeh, K.H.Lin, C.J.Wu, M.D.Tsai, T.L.Li. Structure and Mechanism of A Nonhaem-Iron Sam-Dependent C-Methyltransferase and Its Engineering to A Hydratase and An O-Methyltransferase Acta Crystallogr.,Sect.D V. 70 1549 2014.
ISSN: ISSN 0907-4449
PubMed: 24914966
DOI: 10.1107/S1399004714005239