Magnesium in PDB 9bv1: M2A Midnolin-Proteasome (Translocating)

All present enzymatic activity of M2A Midnolin-Proteasome (Translocating):
3.4.25.1;

The structure of M2A Midnolin-Proteasome (Translocating) also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Magnesium atom in the M2A Midnolin-Proteasome (Translocating) (pdb code 9bv1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the M2A Midnolin-Proteasome (Translocating), PDB code: 9bv1:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the M2A Midnolin-Proteasome (Translocating)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of M2A Midnolin-Proteasome (Translocating) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:34.6 occ:1.00 OG1 A:THR223 2.0 35.0 1.0 O1B A:ATP501 2.3 53.4 1.0 O2G A:ATP501 2.8 53.4 1.0 CB A:THR223 3.1 35.0 1.0 PB A:ATP501 3.4 53.4 1.0 PG A:ATP501 3.5 53.4 1.0 O1G A:ATP501 3.5 53.4 1.0 O3B A:ATP501 3.6 53.4 1.0 O1A A:ATP501 3.8 53.4 1.0 O3A A:ATP501 4.0 53.4 1.0 CG2 A:THR223 4.0 35.0 1.0 N A:THR223 4.1 35.0 1.0 CA A:THR223 4.2 35.0 1.0 OD1 A:ASP275 4.3 39.6 1.0 OD2 A:ASP275 4.3 39.6 1.0 NH2 B:ARG346 4.3 29.4 1.0 PA A:ATP501 4.4 53.4 1.0 O B:ASP317 4.6 32.7 1.0 OE2 A:GLU276 4.7 38.1 1.0 O2B A:ATP501 4.7 53.4 1.0 CG A:ASP275 4.7 39.6 1.0 O3G A:ATP501 4.9 53.4 1.0

Magnesium binding site 2 out of 4 in the M2A Midnolin-Proteasome (Translocating)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of M2A Midnolin-Proteasome (Translocating) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg502 b:27.0 occ:1.00 O2G B:ATP501 2.0 24.1 1.0 O2B B:ATP501 2.3 24.1 1.0 OG1 B:THR233 2.3 30.1 1.0 PG B:ATP501 3.2 24.1 1.0 O3B B:ATP501 3.4 24.1 1.0 PB B:ATP501 3.4 24.1 1.0 OD2 B:ASP285 3.5 27.2 1.0 OD1 B:ASP285 3.6 27.2 1.0 CB B:THR233 3.7 30.1 1.0 O1G B:ATP501 3.8 24.1 1.0 CG B:ASP285 4.0 27.2 1.0 NH2 C:ARG310 4.2 27.5 1.0 O1B B:ATP501 4.4 24.1 1.0 N B:THR233 4.4 30.1 1.0 O3G B:ATP501 4.4 24.1 1.0 CG2 B:THR233 4.4 30.1 1.0 O3A B:ATP501 4.5 24.1 1.0 CA B:THR233 4.6 30.1 1.0 O1A B:ATP501 4.6 24.1 1.0 OE2 B:GLU286 4.8 29.9 1.0 CB B:LYS232 4.9 25.6 1.0 O C:ASP281 4.9 30.8 1.0 CE B:LYS232 5.0 25.6 1.0 CG B:GLU286 5.0 29.9 1.0

Magnesium binding site 3 out of 4 in the M2A Midnolin-Proteasome (Translocating)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of M2A Midnolin-Proteasome (Translocating) within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg502 b:24.2 occ:1.00 O2B C:ATP501 1.9 33.9 1.0 OG1 C:THR197 2.0 28.2 1.0 O1G C:ATP501 3.0 33.9 1.0 CB C:THR197 3.2 28.2 1.0 PB C:ATP501 3.3 33.9 1.0 OD2 C:ASP249 3.3 31.0 1.0 OD1 C:ASP249 3.6 31.0 1.0 O3B C:ATP501 3.8 33.9 1.0 PG C:ATP501 3.9 33.9 1.0 CG C:ASP249 3.9 31.0 1.0 CG2 C:THR197 4.1 28.2 1.0 N C:THR197 4.1 28.2 1.0 O2A C:ATP501 4.2 33.9 1.0 CA C:THR197 4.2 28.2 1.0 O1B C:ATP501 4.2 33.9 1.0 O3A C:ATP501 4.3 33.9 1.0 OE2 C:GLU250 4.6 31.3 1.0 O3G C:ATP501 4.6 33.9 1.0 O D:ASP297 4.6 37.8 1.0 PA C:ATP501 4.7 33.9 1.0

Magnesium binding site 4 out of 4 in the M2A Midnolin-Proteasome (Translocating)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of M2A Midnolin-Proteasome (Translocating) within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg502 b:53.3 occ:1.00 OG1 D:THR213 2.7 43.5 1.0 O1B D:ADP501 3.2 43.1 1.0 O2A D:ADP501 3.3 43.1 1.0 OD1 D:ASP265 3.3 48.4 1.0 OD2 D:ASP265 3.5 48.4 1.0 CB D:THR213 3.7 43.5 1.0 O3B D:ADP501 3.7 43.1 1.0 CG D:ASP265 3.7 48.4 1.0 PB D:ADP501 4.0 43.1 1.0 CG2 D:THR213 4.1 43.5 1.0 OE2 D:GLU266 4.3 50.3 1.0 PA D:ADP501 4.5 43.1 1.0 O3A D:ADP501 4.8 43.1 1.0 CA D:THR213 5.0 43.5 1.0

C.Nardone, X.Gu, J.Gao, M.C.J.Yip, H.Seo, K.Song, L.Sebastian, S.Dhe-Paganon, M.Negasi, N.Kamitaki, M.E.Greenberg, S.J.Elledge, S.Shao. Structural Basis For Nuclear Protein Degradation By the Midnolin-Proteasome Pathway To Be Published.