Magnesium in PDB 5w74: Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State

The structure of Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State, PDB code: 5w74 was solved by K.M.Dalton, T.Lopez, C.Liu, C.Y.Ralston, J.H.Pereira, J.W.Chartron, R.P.Mcandrew, N.R.Douglas, P.D.Adams, V.S.Pande, J.Frydman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.59 / 3.65
Space group	P 21 2 21
Cell size a, b, c (Å), α, β, γ (°)	152.720, 221.930, 262.150, 90.00, 90.00, 90.00
R / Rfree (%)	26.5 / 27.5

The binding sites of Magnesium atom in the Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State (pdb code 5w74). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 8 binding sites of Magnesium where determined in the Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State, PDB code: 5w74:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Magnesium binding site 1 out of 8 in the Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:0.7 occ:1.00 O1B A:ADP600 2.1 0.0 1.0 O3A A:ADP600 2.2 0.8 1.0 PB A:ADP600 2.5 0.6 1.0 PA A:ADP600 2.9 0.3 1.0 O2B A:ADP600 3.0 0.4 1.0 O2A A:ADP600 3.0 0.8 1.0 O1A A:ADP600 3.3 0.2 1.0 OG1 A:THR94 3.6 0.2 1.0 O3B A:ADP600 3.9 0.1 1.0 OD1 A:ASP91 4.0 0.2 1.0 CB A:THR94 4.2 0.8 1.0 O5' A:ADP600 4.4 0.8 1.0 CG A:ASP91 4.8 0.4 1.0 OD2 A:ASP91 4.9 0.7 1.0

Magnesium binding site 2 out of 8 in the Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:0.5 occ:1.00 O3A B:ADP600 2.1 0.8 1.0 OD1 B:ASP91 2.5 0.7 1.0 O1B B:ADP600 3.0 0.1 1.0 PB B:ADP600 3.1 0.7 1.0 O1A B:ADP600 3.2 0.2 1.0 PA B:ADP600 3.2 0.3 1.0 CG B:ASP91 3.4 0.4 1.0 OD2 B:ASP91 3.5 0.2 1.0 O3B B:ADP600 3.6 0.1 1.0 O B:SER157 3.7 1.0 1.0 O5' B:ADP600 4.2 0.8 1.0 O2A B:ADP600 4.3 0.9 1.0 O2B B:ADP600 4.3 0.4 1.0 CE B:LYS161 4.7 0.6 1.0 C5' B:ADP600 4.7 0.5 1.0 CB B:ASP91 4.8 0.2 1.0 C B:SER157 4.9 0.6 1.0

Magnesium binding site 3 out of 8 in the Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg601 b:87.8 occ:1.00 OD1 C:ASP91 2.2 0.3 1.0 O3A C:ADP600 2.5 0.1 1.0 CG C:ASP91 3.0 0.5 1.0 OD2 C:ASP91 3.0 0.2 1.0 O C:SER157 3.4 0.3 1.0 PB C:ADP600 3.4 98.0 1.0 O1B C:ADP600 3.4 0.4 1.0 O3B C:ADP600 3.5 91.4 1.0 PA C:ADP600 3.8 0.7 1.0 O1A C:ADP600 3.8 0.6 1.0 O5' C:ADP600 4.4 98.1 1.0 CB C:ASP91 4.4 0.7 1.0 C C:SER157 4.5 0.1 1.0 CE C:LYS161 4.6 0.6 1.0 OG C:SER157 4.6 0.7 1.0 C5' C:ADP600 4.6 95.8 1.0 O2B C:ADP600 4.8 81.7 1.0 CB C:ALA386 4.9 0.6 1.0 CA C:SER157 4.9 0.9 1.0 O2A C:ADP600 5.0 0.2 1.0

Magnesium binding site 4 out of 8 in the Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg601 b:78.8 occ:1.00 OD1 D:ASP91 2.2 83.0 1.0 O3A D:ADP600 2.3 92.3 1.0 CG D:ASP91 2.9 83.3 1.0 OD2 D:ASP91 3.0 82.8 1.0 O3B D:ADP600 3.2 72.6 1.0 PB D:ADP600 3.2 79.2 1.0 O1B D:ADP600 3.4 94.6 1.0 O D:SER157 3.5 0.6 1.0 PA D:ADP600 3.5 97.9 1.0 O1A D:ADP600 3.6 95.8 1.0 O5' D:ADP600 4.0 79.3 1.0 C5' D:ADP600 4.3 77.0 1.0 CB D:ASP91 4.4 85.4 1.0 C D:SER157 4.5 0.9 1.0 O2B D:ADP600 4.6 63.0 1.0 OG D:SER157 4.6 0.9 1.0 O2A D:ADP600 4.8 0.4 1.0 CA D:SER157 4.8 0.1 1.0 CE D:LYS161 4.8 0.0 1.0 N D:GLY92 4.9 86.5 1.0 CA D:ASP91 5.0 86.8 1.0

Magnesium binding site 5 out of 8 in the Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg601 b:0.4 occ:1.00 O3A E:ADP600 2.0 0.8 1.0 O1B E:ADP600 2.3 0.1 1.0 PB E:ADP600 2.7 0.7 1.0 OD1 E:ASP91 2.9 0.5 1.0 PA E:ADP600 3.1 0.4 1.0 O1A E:ADP600 3.1 0.3 1.0 O3B E:ADP600 3.7 99.1 1.0 O2B E:ADP600 3.8 89.5 1.0 O2A E:ADP600 3.8 0.9 1.0 CG E:ASP91 3.8 0.9 1.0 OD2 E:ASP91 4.0 0.1 1.0 O5' E:ADP600 4.4 0.8 1.0 O E:SER157 4.5 0.1 1.0 OG1 E:THR94 4.6 0.9 1.0 C5' E:ADP600 4.9 0.5 1.0 N E:GLY92 5.0 0.3 1.0

Magnesium binding site 6 out of 8 in the Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg601 b:0.2 occ:1.00 OD1 F:ASP91 2.2 0.1 1.0 O3A F:ADP600 2.3 0.6 1.0 CG F:ASP91 3.0 0.3 1.0 OD2 F:ASP91 3.1 0.5 1.0 PB F:ADP600 3.1 0.5 1.0 O1B F:ADP600 3.1 0.9 1.0 O3B F:ADP600 3.3 0.9 1.0 O F:SER157 3.5 0.2 1.0 PA F:ADP600 3.6 0.2 1.0 O1A F:ADP600 3.7 0.1 1.0 O5' F:ADP600 4.3 0.6 1.0 CB F:ASP91 4.4 1.0 1.0 O2B F:ADP600 4.5 98.2 1.0 C5' F:ADP600 4.5 0.3 1.0 C F:SER157 4.6 0.5 1.0 CE F:LYS161 4.7 0.5 1.0 O2A F:ADP600 4.7 0.7 1.0 OG F:SER157 4.7 0.1 1.0 N F:GLY92 4.9 0.4 1.0

Magnesium binding site 7 out of 8 in the Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ G:Mg601 b:89.5 occ:1.00 OD1 G:ASP91 2.3 0.6 1.0 O3A G:ADP600 2.3 0.7 1.0 O1B G:ADP600 2.9 0.0 1.0 CG G:ASP91 3.1 0.2 1.0 PB G:ADP600 3.1 92.6 1.0 OD2 G:ASP91 3.2 0.4 1.0 O3B G:ADP600 3.5 86.0 1.0 PA G:ADP600 3.6 0.3 1.0 O1A G:ADP600 3.6 0.2 1.0 O G:SER157 3.7 0.0 1.0 O2B G:ADP600 4.4 76.4 1.0 O5' G:ADP600 4.5 92.8 1.0 CB G:ASP91 4.5 0.2 1.0 O2A G:ADP600 4.7 0.8 1.0 C G:SER157 4.8 0.9 1.0 C5' G:ADP600 4.8 90.4 1.0 CE G:LYS161 4.8 0.9 1.0 OG G:SER157 4.9 0.4 1.0 N G:GLY92 5.0 1.0 1.0

Magnesium binding site 8 out of 8 in the Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of Crystal Structure of the Group II Chaperonin From Methanococcus Maripaludis D386ADELTALID Mutant in the Open, Adp-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ H:Mg601 b:84.6 occ:1.00 O3A H:ADP600 2.2 0.3 1.0 OD1 H:ASP91 2.4 92.1 1.0 OD2 H:ASP91 3.0 88.7 1.0 CG H:ASP91 3.0 91.5 1.0 O3B H:ADP600 3.1 80.6 1.0 PB H:ADP600 3.2 87.2 1.0 PA H:ADP600 3.3 0.8 1.0 O H:SER157 3.4 0.3 1.0 O1A H:ADP600 3.4 0.8 1.0 O1B H:ADP600 3.5 0.6 1.0 O5' H:ADP600 3.7 87.3 1.0 C5' H:ADP600 3.9 85.0 1.0 C H:SER157 4.4 0.9 1.0 O2B H:ADP600 4.5 70.9 1.0 CB H:ASP91 4.5 93.5 1.0 O2A H:ADP600 4.6 0.4 1.0 OG H:SER157 4.7 0.8 1.0 CA H:SER157 4.8 0.8 1.0 N H:GLY92 5.0 87.9 1.0

K.M.Dalton, T.Lopez, C.Liu, C.Y.Ralston, J.H.Pereira, J.W.Chartron, R.P.Mcandrew, N.R.Douglas, P.D.Adams, V.S.Pande, J.Frydman. The Conformational Cycle of the Group II Chaperonin Termini To Be Published.