Manganese in PDB 5a1f: Crystal Structure of the Catalytic Domain of PLU1 in Complex with N-Oxalylglycine.

The structure of Crystal Structure of the Catalytic Domain of PLU1 in Complex with N-Oxalylglycine., PDB code: 5a1f was solved by V.Srikannathasan, C.Johansson, C.Strain-Damerell, C.Gileadi, A.Szykowska, K.Kupinska, J.Kopec, T.Krojer, H.Steuber, F.Von Delft, N.A.Burgess-Brown, C.H.Arrowsmith, C.Bountra, A.M.Edwards, U.Oppermann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.01 / 2.10
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	141.855, 141.855, 152.129, 90.00, 90.00, 120.00
R / Rfree (%)	19.931 / 22.501

The structure of Crystal Structure of the Catalytic Domain of PLU1 in Complex with N-Oxalylglycine. also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Manganese atom in the Crystal Structure of the Catalytic Domain of PLU1 in Complex with N-Oxalylglycine. (pdb code 5a1f). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of the Catalytic Domain of PLU1 in Complex with N-Oxalylglycine., PDB code: 5a1f:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of the Catalytic Domain of PLU1 in Complex with N-Oxalylglycine.


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 the Catalytic Domain of PLU1 in Complex with N-Oxalylglycine. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1757 b:85.4 occ:1.00 OD1 A:ASN91 2.6 45.7 1.0 O A:GLU419 2.8 72.1 1.0 O A:THR416 2.8 67.3 1.0 O A:LEU413 2.8 41.0 1.0 O A:LEU90 2.9 43.0 1.0 O A:HOH2042 3.4 56.9 1.0 C A:GLU419 3.7 65.5 1.0 CG A:ASN91 3.8 44.7 1.0 C A:THR416 3.9 66.7 1.0 C A:LEU413 4.0 42.2 1.0 C A:LEU90 4.0 40.9 1.0 O A:VAL414 4.1 38.4 1.0 CB A:GLU419 4.2 71.5 1.0 CA A:VAL414 4.2 39.5 1.0 C A:VAL414 4.2 40.9 1.0 CA A:ASN91 4.4 42.2 1.0 N A:ASP420 4.5 62.6 1.0 CA A:GLU419 4.5 72.1 1.0 N A:THR416 4.5 57.4 1.0 CA A:ASP420 4.5 67.8 1.0 N A:VAL414 4.6 38.6 1.0 CB A:ASN91 4.6 44.2 1.0 N A:ASN91 4.6 42.4 1.0 ND2 A:ASN91 4.7 45.5 1.0 CA A:ILE417 4.7 79.1 1.0 CD1 A:LEU413 4.7 62.9 1.0 N A:ILE417 4.8 74.3 1.0 CA A:THR416 4.8 62.0 1.0 N A:SER415 5.0 45.7 1.0 N A:GLU419 5.0 73.7 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of the Catalytic Domain of PLU1 in Complex with N-Oxalylglycine.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of the Catalytic Domain of PLU1 in Complex with N-Oxalylglycine. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1758 b:29.7 occ:1.00 O A:HOH2098 1.9 30.9 1.0 OE2 A:GLU501 2.1 37.1 1.0 O2' A:OGA1756 2.1 35.7 1.0 NE2 A:HIS587 2.2 32.7 1.0 O1 A:OGA1756 2.2 32.3 1.0 NE2 A:HIS499 2.2 39.6 1.0 C2 A:OGA1756 2.8 35.4 1.0 C1 A:OGA1756 2.8 34.8 1.0 CD A:GLU501 3.0 35.0 1.0 CE1 A:HIS499 3.1 38.8 1.0 CE1 A:HIS587 3.1 32.4 1.0 CD2 A:HIS587 3.2 29.5 1.0 CD2 A:HIS499 3.3 36.5 1.0 OE1 A:GLU501 3.3 34.7 1.0 O2 A:OGA1756 4.1 34.5 1.0 N1 A:OGA1756 4.1 36.4 1.0 OG A:SER507 4.2 38.3 1.0 ND1 A:HIS499 4.2 36.5 1.0 ND1 A:HIS587 4.2 30.1 1.0 CG A:HIS499 4.3 37.1 1.0 CG A:HIS587 4.3 30.2 1.0 O1 A:EDO1766 4.3 48.7 1.0 CG A:GLU501 4.4 35.7 1.0 C1 A:EDO1766 4.7 54.7 1.0 CB A:SER507 4.7 36.3 1.0 C4 A:OGA1756 4.9 38.2 1.0

V.Srikannathasan, C.Johansson, C.Strain-Damerell, C.Gileadi, A.Szykowska, J.Kopec, T.Krojer, H.Steuber, F.Von Delft, N.A.Burgess-Brown, C.H.Arrowsmith, C.Bountra, A.M.Edwards, U.Oppermann. Crystal Structure of PLU1 in Complex with N- Oxalylglycine To Be Published.