Manganese in PDB 1r5g: Crystal Structure of METAP2 Complexed with A311263

All present enzymatic activity of Crystal Structure of METAP2 Complexed with A311263:
3.4.11.18;

The structure of Crystal Structure of METAP2 Complexed with A311263, PDB code: 1r5g was solved by G.S.Sheppard, J.Wang, M.Kawai, N.Y.Bamaung, R.A.Craig, S.A.Erickson, L.Lynch, J.Patel, F.Yang, X.B.Searle, P.Lou, C.Park, K.H.Kim, J.Henkin, R.Lesniewski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.88 / 2.00
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	90.009, 98.612, 101.093, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Manganese atom in the Crystal Structure of METAP2 Complexed with A311263 (pdb code 1r5g). 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 METAP2 Complexed with A311263, PDB code: 1r5g:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of METAP2 Complexed with A311263


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 METAP2 Complexed with A311263 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn480 b:14.0 occ:1.00 OD2 A:ASP262 2.1 12.6 1.0 OE2 A:GLU459 2.2 12.7 1.0 OD1 A:ASP251 2.2 10.6 1.0 OD2 A:ASP251 2.3 10.7 1.0 O24 A:AO1501 2.3 22.1 1.0 CG A:ASP251 2.6 11.2 1.0 N7 A:AO1501 2.6 24.3 1.0 O A:HOH768 2.9 45.3 1.0 CD A:GLU459 3.0 12.7 1.0 CG A:ASP262 3.1 12.9 1.0 OE1 A:GLU459 3.2 12.2 1.0 C8 A:AO1501 3.3 22.7 1.0 OD1 A:ASP262 3.3 13.2 1.0 MN A:MN481 3.4 13.2 1.0 C6 A:AO1501 3.5 23.6 1.0 CZ A:PHE219 3.8 13.6 1.0 OE2 A:GLU364 4.0 12.9 1.0 CB A:ASP251 4.1 11.3 1.0 NE2 A:GLN457 4.2 11.1 1.0 CE2 A:PHE219 4.2 13.4 1.0 O13 A:AO1501 4.3 22.0 1.0 O A:HOH536 4.4 20.7 1.0 CB A:ASP262 4.4 12.9 1.0 CG A:GLU459 4.4 12.5 1.0 C9 A:AO1501 4.5 22.0 1.0 CB A:ALA264 4.7 12.4 1.0 CE1 A:PHE219 4.7 13.5 1.0 N A:CYS263 4.7 12.7 1.0 CD A:GLU364 4.7 13.5 1.0 C A:ASP262 4.7 12.8 1.0 OE1 A:GLU364 4.7 13.2 1.0 CA A:ASP262 4.8 13.0 1.0 C5 A:AO1501 4.8 24.5 1.0 CB A:GLU459 4.9 12.2 1.0 CA A:ASP251 4.9 11.7 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of METAP2 Complexed with A311263


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 METAP2 Complexed with A311263 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn481 b:13.2 occ:1.00 OD1 A:ASP262 2.1 13.2 1.0 OE1 A:GLU364 2.2 13.2 1.0 OE1 A:GLU459 2.2 12.2 1.0 O24 A:AO1501 2.2 22.1 1.0 O13 A:AO1501 2.3 22.0 1.0 NE2 A:HIS331 2.4 14.3 1.0 C9 A:AO1501 2.9 22.0 1.0 C8 A:AO1501 2.9 22.7 1.0 CG A:ASP262 3.0 12.9 1.0 CD A:GLU364 3.0 13.5 1.0 CD A:GLU459 3.2 12.7 1.0 CD2 A:HIS331 3.3 14.3 1.0 OE2 A:GLU364 3.3 12.9 1.0 C6 A:AO1501 3.4 23.6 1.0 MN A:MN480 3.4 14.0 1.0 CE1 A:HIS331 3.4 14.2 1.0 OD2 A:ASP262 3.5 12.6 1.0 OE2 A:GLU459 3.6 12.7 1.0 N7 A:AO1501 3.7 24.3 1.0 CB A:ALA362 3.9 15.4 1.0 N10 A:AO1501 4.0 21.2 1.0 CB A:ASP262 4.2 12.9 1.0 CG A:GLU364 4.3 13.3 1.0 CG A:HIS331 4.5 14.6 1.0 ND1 A:HIS331 4.5 14.3 1.0 CG A:GLU459 4.5 12.5 1.0 C11 A:AO1501 4.7 21.0 1.0 CD1 A:ILE338 4.7 18.9 1.0 C5 A:AO1501 4.8 24.5 1.0 CE1 A:HIS339 4.8 20.5 1.0 CB A:GLU364 5.0 13.4 1.0

G.S.Sheppard, J.Wang, M.Kawai, N.Y.Bamaung, R.A.Craig, S.A.Erickson, L.Lynch, J.Patel, F.Yang, X.B.Searle, P.Lou, C.Park, K.H.Kim, J.Henkin, R.Lesniewski. 3-Amino-2-Hydroxyamides and Related Compounds As Inhibitors of Methionine Aminopeptidase-2. Bioorg.Med.Chem.Lett. V. 14 865 2004.
ISSN: ISSN 0960-894X
PubMed: 15012983
DOI: 10.1016/J.BMCL.2003.12.031