Manganese in PDB 3pkx: Crystal Structure of Toxoflavin Lyase (Tfla) Bound to Mn(II) and Toxoflavin

The structure of Crystal Structure of Toxoflavin Lyase (Tfla) Bound to Mn(II) and Toxoflavin, PDB code: 3pkx was solved by M.K.Fenwick, B.Philmus, T.P.Begley, S.E.Ealick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.80 / 1.50
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	111.195, 111.195, 57.067, 90.00, 90.00, 120.00
R / Rfree (%)	20.6 / 23

The binding sites of Manganese atom in the Crystal Structure of Toxoflavin Lyase (Tfla) Bound to Mn(II) and Toxoflavin (pdb code 3pkx). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of Toxoflavin Lyase (Tfla) Bound to Mn(II) and Toxoflavin, PDB code: 3pkx:

Manganese binding site 1 out of 1 in the Crystal Structure of Toxoflavin Lyase (Tfla) Bound to Mn(II) and Toxoflavin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Toxoflavin Lyase (Tfla) Bound to Mn(II) and Toxoflavin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn230 b:17.2 occ:1.00 OE2 A:GLU138 2.1 16.9 1.0 OE1 A:GLU113 2.1 17.2 1.0 O1 A:TOF231 2.2 17.6 1.0 O A:HOH404 2.2 17.8 1.0 NE2 A:HIS60 2.2 15.4 1.0 C1 A:TOF231 3.0 21.0 1.0 CD A:GLU138 3.1 19.4 1.0 CE1 A:HIS60 3.1 16.4 1.0 CD A:GLU113 3.1 15.4 1.0 CD2 A:HIS60 3.3 16.7 1.0 OE2 A:GLU113 3.4 17.4 1.0 OE1 A:GLU138 3.4 19.2 1.0 N3 A:TOF231 3.7 20.1 1.0 C2 A:TOF231 3.8 18.3 1.0 OH A:TYR103 3.9 18.3 1.0 N10 A:TOF231 4.0 22.9 1.0 CD1 A:LEU181 4.1 30.2 1.0 C12 A:TOF231 4.2 18.0 1.0 ND1 A:HIS60 4.3 17.3 1.0 CE2 A:TYR103 4.4 15.1 1.0 CG A:GLU138 4.4 17.8 1.0 CB A:ALA62 4.4 14.7 1.0 CG A:HIS60 4.4 16.6 1.0 CG A:GLU113 4.5 14.5 1.0 CZ A:TYR103 4.6 16.1 1.0 CB A:GLU138 4.7 17.4 1.0 CB A:GLU113 4.7 15.9 1.0 C4 A:TOF231 5.0 27.0 1.0

M.K.Fenwick, B.Philmus, T.P.Begley, S.E.Ealick. Toxoflavin Lyase Requires A Novel 1-His-2-Carboxylate Facial Triad . Biochemistry V. 50 1091 2011.
ISSN: ISSN 0006-2960
PubMed: 21166463
DOI: 10.1021/BI101741V