Manganese in PDB 2ea4: H-METAP2 Complexed with A797859

All present enzymatic activity of H-METAP2 Complexed with A797859:
3.4.11.18;

The structure of H-METAP2 Complexed with A797859, PDB code: 2ea4 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)	19.63 / 2.35
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	90.091, 100.280, 100.722, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of H-METAP2 Complexed with A797859 also contains other interesting chemical elements:

Fluorine

(F)

1 atom

The binding sites of Manganese atom in the H-METAP2 Complexed with A797859 (pdb code 2ea4). 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 A797859, PDB code: 2ea4:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the H-METAP2 Complexed with A797859


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 A797859 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn480 b:33.7 occ:1.00 OD2 A:ASP251 2.2 20.0 1.0 OD2 A:ASP262 2.3 23.1 1.0 OE2 A:GLU459 2.4 21.7 1.0 OD1 A:ASP251 2.5 20.2 1.0 N12 A:F79482 2.5 32.1 1.0 CG A:ASP251 2.7 19.9 1.0 CG A:ASP262 3.1 23.1 1.0 CD A:GLU459 3.2 21.8 1.0 OD1 A:ASP262 3.3 23.4 1.0 MN A:MN481 3.4 30.6 1.0 OE1 A:GLU459 3.4 21.9 1.0 C11 A:F79482 3.4 32.5 1.0 OE2 A:GLU364 4.1 22.9 1.0 CB A:ASP251 4.2 19.4 1.0 CZ A:PHE219 4.2 18.4 1.0 O14 A:F79482 4.2 33.7 1.0 NE2 A:GLN457 4.2 20.5 1.0 O15 A:F79482 4.3 33.6 1.0 CE2 A:PHE219 4.4 18.3 1.0 CB A:ALA264 4.5 20.8 1.0 CB A:ASP262 4.6 22.8 1.0 C13 A:F79482 4.6 33.8 1.0 O A:HOH761 4.6 52.6 1.0 CG A:GLU459 4.7 21.8 1.0 C10 A:F79482 4.8 32.8 1.0 CD A:GLU364 4.9 22.9 1.0 N A:CYS263 5.0 22.1 1.0 CA A:ASP262 5.0 22.6 1.0

Manganese binding site 2 out of 2 in the H-METAP2 Complexed with A797859


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 A797859 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn481 b:30.6 occ:1.00 O14 A:F79482 2.1 33.7 1.0 OE1 A:GLU459 2.2 21.9 1.0 OD1 A:ASP262 2.4 23.4 1.0 OE1 A:GLU364 2.6 22.8 1.0 NE2 A:HIS331 2.6 23.2 1.0 CD A:GLU364 3.2 22.9 1.0 CD A:GLU459 3.2 21.8 1.0 C13 A:F79482 3.3 33.8 1.0 CD2 A:HIS331 3.3 23.3 1.0 CG A:ASP262 3.3 23.1 1.0 OE2 A:GLU364 3.4 22.9 1.0 MN A:MN480 3.4 33.7 1.0 O15 A:F79482 3.6 33.6 1.0 OE2 A:GLU459 3.6 21.7 1.0 CE1 A:HIS331 3.7 23.2 1.0 OD2 A:ASP262 3.7 23.1 1.0 CB A:ALA362 3.9 26.0 1.0 N12 A:F79482 4.2 32.1 1.0 CG A:GLU364 4.4 22.9 1.0 C11 A:F79482 4.4 32.5 1.0 CB A:ASP262 4.5 22.8 1.0 C2 A:F79482 4.5 34.0 1.0 CG A:GLU459 4.5 21.8 1.0 CG A:HIS331 4.6 23.5 1.0 C21 A:F79482 4.6 37.0 1.0 ND1 A:HIS331 4.7 23.2 1.0 N16 A:F79482 4.8 35.6 1.0 C22 A:F79482 5.0 37.1 1.0

G.T.Wang, R.A.Mantei, M.Kawai, J.S.Tedrow, D.M.Barnes, J.Wang, Q.Zhang, P.Lou, L.A.Garcia, J.Bouska, M.Yates, C.Park, R.A.Judge, R.Lesniewski, G.S.Sheppard, R.L.Bell. Lead Optimization of Methionine Aminopeptidase-2 (METAP2) Inhibitors Containing Sulfonamides of 5,6-Disubstituted Anthranilic Acids Bioorg.Med.Chem.Lett. V. 17 2817 2007.
ISSN: ISSN 0960-894X
PubMed: 17350258
DOI: 10.1016/J.BMCL.2007.02.062