Cobalt in PDB 2oaz: Human Methionine Aminopeptidase-2 Complexed with Sb-587094

All present enzymatic activity of Human Methionine Aminopeptidase-2 Complexed with Sb-587094:
3.4.11.18;

The structure of Human Methionine Aminopeptidase-2 Complexed with Sb-587094, PDB code: 2oaz was solved by J.P.Marino Jr., P.W.Fisher, G.A.Hofmann, R.Kirkpatrick, C.A.Janson, R.K.Johnson, C.Ma, M.Mattern, T.D.Meek, D.Ryan, C.Schulz, W.W.Smith, D.G.Tew, T.A.Tomazek Jr., D.F.Veber, W.C.Xiong, Y.Yamamoto, K.Yamashita, G.Yang, S.K.Thompson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.90
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	89.698, 99.217, 101.304, 90.00, 90.00, 90.00
R / Rfree (%)	25.5 / 28.7

The binding sites of Cobalt atom in the Human Methionine Aminopeptidase-2 Complexed with Sb-587094 (pdb code 2oaz). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Human Methionine Aminopeptidase-2 Complexed with Sb-587094, PDB code: 2oaz:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Human Methionine Aminopeptidase-2 Complexed with Sb-587094


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Human Methionine Aminopeptidase-2 Complexed with Sb-587094 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co479 b:24.6 occ:1.00 OD1 A:ASP262 1.8 39.8 1.0 OE1 A:GLU459 1.9 40.9 1.0 OD2 A:ASP251 2.1 33.3 1.0 N15 A:I96501 2.3 53.0 1.0 OD1 A:ASP251 2.4 33.6 1.0 CG A:ASP251 2.6 33.2 1.0 CG A:ASP262 2.7 40.8 1.0 OD2 A:ASP262 2.9 39.8 1.0 CD A:GLU459 2.9 41.5 1.0 CO A:CO480 3.1 28.6 1.0 OE2 A:GLU459 3.2 39.8 1.0 C14 A:I96501 3.2 53.3 1.0 N13 A:I96501 3.3 52.8 1.0 S16 A:I96501 3.5 48.6 1.0 CZ A:PHE219 3.9 38.8 1.0 CB A:ASP251 4.1 36.4 1.0 CB A:ASP262 4.1 39.9 1.0 CG A:GLU459 4.3 41.4 1.0 OE2 A:GLU364 4.3 43.4 1.0 OE1 A:GLU364 4.3 43.7 1.0 C7 A:I96501 4.4 53.2 1.0 NE2 A:GLN457 4.4 35.2 1.0 CE1 A:PHE219 4.4 39.3 1.0 N12 A:I96501 4.4 52.6 1.0 CD A:GLU364 4.6 43.3 1.0 C A:ASP262 4.6 40.9 1.0 CA A:ASP262 4.6 40.8 1.0 N A:CYS263 4.7 39.7 1.0 CB A:ALA264 4.7 38.6 1.0 CE2 A:PHE219 4.7 38.8 1.0 CB A:GLU459 4.8 40.0 1.0

Cobalt binding site 2 out of 2 in the Human Methionine Aminopeptidase-2 Complexed with Sb-587094


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Human Methionine Aminopeptidase-2 Complexed with Sb-587094 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co480 b:28.6 occ:1.00 OE2 A:GLU459 1.9 39.8 1.0 OD2 A:ASP262 1.9 39.8 1.0 OE2 A:GLU364 2.1 43.4 1.0 NE2 A:HIS331 2.2 43.2 1.0 N13 A:I96501 2.5 52.8 1.0 CD A:GLU459 2.9 41.5 1.0 N15 A:I96501 2.9 53.0 1.0 CG A:ASP262 3.0 40.8 1.0 CD A:GLU364 3.1 43.3 1.0 CO A:CO479 3.1 24.6 1.0 CD2 A:HIS331 3.2 44.2 1.0 OE1 A:GLU459 3.2 40.9 1.0 CE1 A:HIS331 3.2 43.6 1.0 C7 A:I96501 3.5 53.2 1.0 OD1 A:ASP262 3.5 39.8 1.0 OE1 A:GLU364 3.7 43.7 1.0 CB A:ALA362 3.8 40.3 1.0 N3 A:I96501 3.9 52.6 1.0 C14 A:I96501 3.9 53.3 1.0 CG A:GLU364 4.1 42.5 1.0 CB A:ASP262 4.2 39.9 1.0 N12 A:I96501 4.3 52.6 1.0 CG A:GLU459 4.3 41.4 1.0 ND1 A:HIS331 4.3 43.5 1.0 CG A:HIS331 4.4 44.1 1.0 OD2 A:ASP251 4.7 33.3 1.0 CB A:GLU364 4.8 41.8 1.0 CD1 A:ILE338 4.9 49.6 1.0

J.P.Marino, P.W.Fisher, G.A.Hofmann, R.B.Kirkpatrick, C.A.Janson, R.K.Johnson, C.Ma, M.Mattern, T.D.Meek, M.D.Ryan, C.Schulz, W.W.Smith, D.G.Tew, T.A.Tomazek, D.F.Veber, W.C.Xiong, Y.Yamamoto, K.Yamashita, G.Yang, S.K.Thompson. Highly Potent Inhibitors of Methionine Aminopeptidase-2 Based on A 1,2,4-Triazole Pharmacophore. J.Med.Chem. V. 50 3777 2007.
ISSN: ISSN 0022-2623
PubMed: 17636946
DOI: 10.1021/JM061182W