Cobalt in PDB 1bn5: Human Methionine Aminopeptidase 2

All present enzymatic activity of Human Methionine Aminopeptidase 2:
3.4.11.18;

The structure of Human Methionine Aminopeptidase 2, PDB code: 1bn5 was solved by S.Liu, J.Widom, C.W.Kemp, C.M.Crews, J.C.Clardy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.80
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	90.490, 99.380, 101.590, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 22.8

The binding sites of Cobalt atom in the Human Methionine Aminopeptidase 2 (pdb code 1bn5). 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, PDB code: 1bn5:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Human Methionine Aminopeptidase 2


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co479 b:41.9 occ:1.00 OD1 A:ASP262 2.0 25.8 1.0 OE1 A:GLU459 2.3 21.7 1.0 OD2 A:ASP251 2.4 21.3 1.0 OD1 A:ASP251 2.4 20.1 1.0 CG A:ASP251 2.7 19.2 1.0 CG A:ASP262 2.8 25.9 1.0 OD2 A:ASP262 2.9 29.5 1.0 CD A:GLU459 3.1 20.2 1.0 CO A:CO480 3.1 49.4 1.0 OE2 A:GLU459 3.2 20.9 1.0 O A:HOH643 4.0 31.0 1.0 CZ A:PHE219 4.0 14.9 1.0 NE2 A:GLN457 4.2 15.3 1.0 OE1 A:GLU364 4.2 29.9 1.0 CB A:ASP262 4.2 20.3 1.0 CB A:ASP251 4.2 15.2 1.0 O A:HOH626 4.3 29.5 1.0 CE1 A:PHE219 4.4 14.6 1.0 OE2 A:GLU364 4.5 33.8 1.0 CG A:GLU459 4.6 14.7 1.0 CB A:ALA264 4.6 12.7 1.0 N A:CYS263 4.6 13.1 1.0 C A:ASP262 4.6 12.9 1.0 CA A:ASP262 4.7 17.8 1.0 CD A:GLU364 4.7 31.6 1.0 O A:HOH666 4.7 43.7 1.0 CE2 A:PHE219 4.8 15.9 1.0 O A:HOH700 5.0 37.9 1.0

Cobalt binding site 2 out of 2 in the Human Methionine Aminopeptidase 2


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co480 b:49.4 occ:1.00 OE2 A:GLU364 2.2 33.8 1.0 OD2 A:ASP262 2.3 29.5 1.0 OE2 A:GLU459 2.4 20.9 1.0 NE2 A:HIS331 2.4 25.5 1.0 CD A:GLU364 3.1 31.6 1.0 CO A:CO479 3.1 41.9 1.0 O A:HOH666 3.1 43.7 1.0 CG A:ASP262 3.2 25.9 1.0 CD2 A:HIS331 3.3 25.8 1.0 CE1 A:HIS331 3.4 24.4 1.0 CD A:GLU459 3.4 20.2 1.0 OE1 A:GLU364 3.5 29.9 1.0 OD1 A:ASP262 3.6 25.8 1.0 OE1 A:GLU459 3.8 21.7 1.0 CB A:ALA362 4.0 15.4 1.0 O A:HOH643 4.2 31.0 1.0 CB A:ASP262 4.2 20.3 1.0 CG A:GLU364 4.3 28.6 1.0 ND1 A:HIS331 4.5 24.9 1.0 CG A:HIS331 4.5 24.3 1.0 CG A:GLU459 4.7 14.7 1.0 CB A:GLU364 4.9 24.8 1.0 OD2 A:ASP251 5.0 21.3 1.0

S.Liu, J.Widom, C.W.Kemp, C.M.Crews, J.Clardy. Structure of Human Methionine Aminopeptidase-2 Complexed with Fumagillin. Science V. 282 1324 1998.
ISSN: ISSN 0036-8075
PubMed: 9812898
DOI: 10.1126/SCIENCE.282.5392.1324