Manganese in PDB 1yw8: H-METAP2 Complexed with A751277

All present enzymatic activity of H-METAP2 Complexed with A751277:
3.4.11.18;

The structure of H-METAP2 Complexed with A751277, PDB code: 1yw8 was solved by C.H.Park, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.98 / 2.65
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	89.527, 99.225, 101.191, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Manganese atom in the H-METAP2 Complexed with A751277 (pdb code 1yw8). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the H-METAP2 Complexed with A751277, PDB code: 1yw8:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the H-METAP2 Complexed with A751277


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of H-METAP2 Complexed with A751277 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn480 b:18.7 occ:1.00 OD1 A:ASP251 2.2 15.4 1.0 OD2 A:ASP262 2.2 19.2 1.0 OE2 A:GLU459 2.2 18.5 1.0 OD2 A:ASP251 2.4 15.7 1.0 CG A:ASP251 2.6 15.3 1.0 CG A:ASP262 3.0 19.2 1.0 OD1 A:ASP262 3.1 19.0 1.0 CD A:GLU459 3.1 18.7 1.0 MN A:MN481 3.3 19.3 1.0 OE1 A:GLU459 3.4 18.5 1.0 OE2 A:GLU364 3.9 19.9 1.0 CZ A:PHE219 3.9 15.0 1.0 CB A:ASP251 4.0 15.2 1.0 O13 A:A75104 4.1 33.8 1.0 CE2 A:PHE219 4.1 14.8 1.0 O12 A:A75104 4.2 33.7 1.0 NE2 A:GLN457 4.3 18.5 1.0 CB A:ASP262 4.4 19.4 1.0 C11 A:A75104 4.5 33.7 1.0 O A:HOH24 4.5 29.9 1.0 CG A:GLU459 4.5 18.4 1.0 O A:HOH65 4.7 47.8 1.0 CB A:ALA264 4.7 17.6 1.0 CD A:GLU364 4.7 20.1 1.0 N A:CYS263 4.8 18.8 1.0 C A:ASP262 4.8 19.0 1.0 CA A:ASP262 4.8 19.3 1.0 CE1 A:PHE219 4.9 15.1 1.0 CA A:ASP251 4.9 14.9 1.0 OE1 A:GLU364 4.9 20.5 1.0 CB A:GLU459 4.9 18.4 1.0

Manganese binding site 2 out of 2 in the H-METAP2 Complexed with A751277


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of H-METAP2 Complexed with A751277 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn481 b:19.3 occ:1.00 OD1 A:ASP262 2.1 19.0 1.0 OE1 A:GLU459 2.2 18.5 1.0 NE2 A:HIS331 2.3 22.1 1.0 O12 A:A75104 2.4 33.7 1.0 OE1 A:GLU364 2.4 20.5 1.0 CD A:GLU364 3.1 20.1 1.0 CD2 A:HIS331 3.1 22.1 1.0 OE2 A:GLU364 3.1 19.9 1.0 CG A:ASP262 3.2 19.2 1.0 CD A:GLU459 3.2 18.7 1.0 MN A:MN480 3.3 18.7 1.0 C11 A:A75104 3.3 33.7 1.0 CE1 A:HIS331 3.4 22.0 1.0 O13 A:A75104 3.5 33.8 1.0 OE2 A:GLU459 3.5 18.5 1.0 OD2 A:ASP262 3.7 19.2 1.0 CB A:ALA362 4.2 22.4 1.0 C23 A:A75104 4.2 34.2 1.0 CG A:HIS331 4.3 22.1 1.0 CB A:ASP262 4.4 19.4 1.0 ND1 A:HIS331 4.4 22.1 1.0 CG A:GLU364 4.5 20.2 1.0 CG A:GLU459 4.5 18.4 1.0 C22 A:A75104 4.7 34.2 1.0 C10 A:A75104 4.8 33.7 1.0 N14 A:A75104 4.8 34.2 1.0 CB A:GLU364 5.0 20.1 1.0

G.S.Sheppard, J.Wang, M.Kawai, S.D.Fidanze, N.Y.Bamaung, S.A.Erickson, D.M.Barnes, J.S.Tedrow, L.Kolaczkowski, A.Vasudevan, D.C.Park, G.T.Wang, W.J.Sanders, R.A.Mantei, F.Palazzo, L.Tucker-Garcia, P.Lou, Q.Zhang, C.H.Park, K.H.Kim, A.Petros, E.Olejniczak, D.Nettesheim, P.Hajduk, J.Henkin, R.Lesniewski, S.K.Davidsen, R.L.Bell. Discovery and Optimization of Anthranilic Acid Sulfonamides As Inhibitors of Methionine Aminopeptidase-2: A Structural Basis For the Reduction of Albumin Binding. J.Med.Chem. V. 49 3832 2006.
ISSN: ISSN 0022-2623
PubMed: 16789740
DOI: 10.1021/JM0601001