Magnesium in PDB 1kp8: Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution

The structure of Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution, PDB code: 1kp8 was solved by J.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.89 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	135.571, 260.112, 150.200, 90.00, 101.14, 90.00
R / Rfree (%)	24.3 / 25.8

The structure of Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution also contains other interesting chemical elements:

Potassium

(K)

16 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 14;

Binding sites:

The binding sites of Magnesium atom in the Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution (pdb code 1kp8). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 14 binding sites of Magnesium where determined in the Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution, PDB code: 1kp8:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 14 in the Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg550 b:31.5 occ:1.00 O A:HOH5433 1.9 50.8 1.0 O3G A:AGS1 2.2 42.2 1.0 OD1 A:ASP87 2.2 52.9 1.0 O A:HOH5432 2.3 45.0 1.0 O2A A:AGS1 2.4 36.8 1.0 O1B A:AGS1 2.4 35.9 1.0 CG A:ASP87 3.3 50.0 1.0 PB A:AGS1 3.5 36.3 1.0 PG A:AGS1 3.5 44.1 1.0 PA A:AGS1 3.6 36.6 1.0 OD2 A:ASP87 3.6 52.1 1.0 O3A A:AGS1 3.8 36.9 1.0 O3B A:AGS1 3.9 38.8 1.0 O2G A:AGS1 4.0 39.8 1.0 O A:HOH5019 4.1 36.4 1.0 O A:HOH5463 4.1 50.1 1.0 N A:GLY88 4.4 41.8 1.0 C5' A:AGS1 4.5 36.8 1.0 O5' A:AGS1 4.5 35.1 1.0 CB A:ASP87 4.6 46.1 1.0 S1G A:AGS1 4.7 41.0 1.0 O1A A:AGS1 4.7 37.3 1.0 O A:HOH5014 4.7 54.6 1.0 O A:HOH5013 4.8 82.5 1.0 O2B A:AGS1 4.8 35.5 1.0 CA A:ASP87 4.9 43.8 1.0

Magnesium binding site 2 out of 14 in the Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg550 b:31.7 occ:1.00 O B:HOH5435 2.0 66.8 1.0 O1B B:AGS1 2.2 38.8 1.0 O2A B:AGS1 2.2 39.3 1.0 O3G B:AGS1 2.3 48.2 1.0 OD1 B:ASP87 2.3 47.7 1.0 O B:HOH5434 2.4 42.6 1.0 CG B:ASP87 3.2 48.0 1.0 PB B:AGS1 3.3 40.8 1.0 OD2 B:ASP87 3.3 50.5 1.0 PA B:AGS1 3.4 38.7 1.0 PG B:AGS1 3.5 50.2 1.0 O3A B:AGS1 3.6 39.0 1.0 O3B B:AGS1 3.8 44.5 1.0 O B:HOH5050 3.9 40.2 1.0 O2G B:AGS1 4.1 48.8 1.0 C5' B:AGS1 4.1 38.0 1.0 O5' B:AGS1 4.2 40.6 1.0 O B:HOH5467 4.3 39.5 1.0 O B:HOH5044 4.4 57.2 1.0 N B:GLY88 4.4 38.6 1.0 O1A B:AGS1 4.6 36.0 1.0 CB B:ASP87 4.6 44.1 1.0 O2B B:AGS1 4.6 43.0 1.0 O B:HOH2602 4.7 70.4 1.0 S1G B:AGS1 4.7 45.6 1.0

Magnesium binding site 3 out of 14 in the Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg550 b:36.8 occ:1.00 O C:HOH5437 2.0 68.2 1.0 O C:HOH5436 2.2 44.4 1.0 O3G C:AGS1 2.2 49.1 1.0 O2A C:AGS1 2.2 41.7 1.0 OD1 C:ASP87 2.3 50.2 1.0 O1B C:AGS1 2.5 49.4 1.0 CG C:ASP87 3.3 50.4 1.0 PA C:AGS1 3.5 40.4 1.0 PB C:AGS1 3.5 44.4 1.0 PG C:AGS1 3.5 52.1 1.0 OD2 C:ASP87 3.6 51.5 1.0 O3A C:AGS1 3.7 42.1 1.0 O3B C:AGS1 3.9 48.0 1.0 O2G C:AGS1 4.1 46.8 1.0 O C:HOH5471 4.1 39.1 1.0 O C:HOH5081 4.2 50.3 1.0 O C:HOH5075 4.2 56.7 1.0 C5' C:AGS1 4.4 40.8 1.0 O5' C:AGS1 4.4 41.7 1.0 N C:GLY88 4.5 46.1 1.0 O1A C:AGS1 4.6 37.5 1.0 S1G C:AGS1 4.7 47.7 1.0 CB C:ASP87 4.7 48.8 1.0 O2B C:AGS1 4.9 47.8 1.0

Magnesium binding site 4 out of 14 in the Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg550 b:29.1 occ:1.00 O D:HOH5439 2.0 52.0 1.0 O2A D:AGS551 2.2 32.2 1.0 O3G D:AGS551 2.2 39.7 1.0 O1B D:AGS551 2.3 33.4 1.0 OD1 D:ASP87 2.3 44.8 1.0 O D:HOH5438 2.6 46.7 1.0 CG D:ASP87 3.3 41.5 1.0 PB D:AGS551 3.4 31.0 1.0 PA D:AGS551 3.4 31.6 1.0 PG D:AGS551 3.5 41.1 1.0 OD2 D:ASP87 3.6 44.3 1.0 O3A D:AGS551 3.6 31.2 1.0 O3B D:AGS551 3.8 34.5 1.0 O D:HOH5475 3.9 34.0 1.0 O2G D:AGS551 4.1 39.2 1.0 O D:HOH5112 4.1 34.0 1.0 O D:HOH5106 4.2 78.1 1.0 O5' D:AGS551 4.3 33.1 1.0 C5' D:AGS551 4.3 33.4 1.0 N D:GLY88 4.4 32.2 1.0 O1A D:AGS551 4.5 33.3 1.0 S1G D:AGS551 4.6 40.5 1.0 O2B D:AGS551 4.7 32.3 1.0 CB D:ASP87 4.7 37.8 1.0

Magnesium binding site 5 out of 14 in the Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg550 b:24.5 occ:1.00 O E:HOH5441 2.0 48.1 1.0 O2A E:AGS1 2.2 29.8 1.0 O E:HOH5440 2.2 42.5 1.0 O3G E:AGS1 2.2 32.5 1.0 O1B E:AGS1 2.3 32.1 1.0 OD1 E:ASP87 2.3 41.1 1.0 CG E:ASP87 3.3 41.2 1.0 PB E:AGS1 3.3 31.9 1.0 PA E:AGS1 3.3 31.4 1.0 PG E:AGS1 3.5 37.1 1.0 O3A E:AGS1 3.6 32.9 1.0 OD2 E:ASP87 3.6 44.8 1.0 O3B E:AGS1 3.8 33.2 1.0 O E:HOH5479 4.0 31.7 1.0 O2G E:AGS1 4.1 34.5 1.0 O E:HOH2209 4.1 56.0 1.0 O E:HOH5143 4.1 35.1 1.0 O5' E:AGS1 4.2 31.4 1.0 C5' E:AGS1 4.2 30.3 1.0 N E:GLY88 4.4 31.4 1.0 O1A E:AGS1 4.5 32.0 1.0 S1G E:AGS1 4.6 35.3 1.0 O2B E:AGS1 4.7 30.1 1.0 CB E:ASP87 4.7 36.5 1.0 O E:HOH1953 4.9 53.3 1.0

Magnesium binding site 6 out of 14 in the Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg550 b:30.4 occ:1.00 O3G F:AGS1 2.1 45.6 1.0 O F:HOH5442 2.2 51.2 1.0 O2A F:AGS1 2.3 37.5 1.0 O F:HOH2845 2.3 66.7 1.0 OD1 F:ASP87 2.4 50.7 1.0 O1B F:AGS1 2.4 44.7 1.0 O F:HOH5443 3.0 63.1 1.0 CG F:ASP87 3.4 51.5 1.0 PB F:AGS1 3.4 38.0 1.0 PG F:AGS1 3.4 45.8 1.0 PA F:AGS1 3.4 34.9 1.0 OD2 F:ASP87 3.7 54.4 1.0 O3A F:AGS1 3.7 38.9 1.0 O3B F:AGS1 3.8 40.3 1.0 O2G F:AGS1 4.0 42.0 1.0 O F:HOH5483 4.1 35.6 1.0 O F:HOH1546 4.2 54.4 1.0 O5' F:AGS1 4.3 37.8 1.0 C5' F:AGS1 4.3 35.8 1.0 O F:HOH5174 4.4 36.6 1.0 N F:GLY88 4.5 42.6 1.0 S1G F:AGS1 4.6 44.7 1.0 O1A F:AGS1 4.6 40.5 1.0 CB F:ASP87 4.7 47.8 1.0 O2B F:AGS1 4.8 40.1 1.0 O F:HOH2498 4.8 73.9 1.0

Magnesium binding site 7 out of 14 in the Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ G:Mg550 b:29.9 occ:1.00 O G:HOH5445 2.1 51.7 1.0 O2A G:AGS1 2.2 36.5 1.0 O3G G:AGS1 2.3 41.3 1.0 OD1 G:ASP87 2.4 47.5 1.0 O G:HOH5444 2.4 50.7 1.0 O1B G:AGS1 2.4 37.7 1.0 CG G:ASP87 3.4 46.3 1.0 PA G:AGS1 3.4 34.9 1.0 PB G:AGS1 3.4 33.8 1.0 PG G:AGS1 3.5 41.1 1.0 OD2 G:ASP87 3.6 48.3 1.0 O3A G:AGS1 3.7 36.0 1.0 O3B G:AGS1 3.9 37.2 1.0 O G:HOH5199 4.0 59.7 1.0 O2G G:AGS1 4.1 40.2 1.0 O G:HOH5487 4.1 36.3 1.0 O G:HOH5205 4.2 29.3 1.0 O5' G:AGS1 4.3 34.1 1.0 C5' G:AGS1 4.3 33.4 1.0 N G:GLY88 4.5 38.7 1.0 O1A G:AGS1 4.5 38.7 1.0 S1G G:AGS1 4.7 40.7 1.0 CB G:ASP87 4.8 44.1 1.0 O G:HOH2616 4.8 69.0 1.0 O2B G:AGS1 4.8 35.0 1.0

Magnesium binding site 8 out of 14 in the Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ H:Mg550 b:27.0 occ:1.00 O H:HOH5446 2.1 39.5 1.0 O H:HOH5447 2.1 48.7 1.0 O2A H:AGS1 2.2 35.4 1.0 O3G H:AGS1 2.2 37.5 1.0 O1B H:AGS1 2.3 34.7 1.0 OD1 H:ASP87 2.3 47.4 1.0 PB H:AGS1 3.3 33.0 1.0 CG H:ASP87 3.3 47.8 1.0 PA H:AGS1 3.3 35.3 1.0 PG H:AGS1 3.5 42.0 1.0 O3A H:AGS1 3.5 35.6 1.0 OD2 H:ASP87 3.6 51.0 1.0 O3B H:AGS1 3.7 37.3 1.0 O H:HOH5491 4.0 38.4 1.0 O H:HOH2994 4.0 80.7 1.0 O2G H:AGS1 4.0 38.5 1.0 O H:HOH5236 4.1 37.7 1.0 O H:HOH1741 4.1 60.5 1.0 C5' H:AGS1 4.2 35.4 1.0 O5' H:AGS1 4.2 37.4 1.0 N H:GLY88 4.3 36.9 1.0 O1A H:AGS1 4.5 35.5 1.0 O H:HOH2950 4.6 86.9 1.0 S1G H:AGS1 4.6 40.4 1.0 O2B H:AGS1 4.6 35.5 1.0 O H:HOH1484 4.7 49.3 1.0 CB H:ASP87 4.7 42.7 1.0 CA H:ASP87 5.0 41.7 1.0

Magnesium binding site 9 out of 14 in the Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 9 of Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ I:Mg550 b:34.5 occ:1.00 O I:HOH5449 2.0 52.3 1.0 O I:HOH5448 2.0 48.4 1.0 O3G I:AGS1 2.3 51.7 1.0 O2A I:AGS1 2.3 41.2 1.0 OD1 I:ASP87 2.4 54.9 1.0 O1B I:AGS1 2.4 45.3 1.0 CG I:ASP87 3.3 53.9 1.0 PB I:AGS1 3.5 42.5 1.0 PA I:AGS1 3.6 41.8 1.0 PG I:AGS1 3.6 50.6 1.0 OD2 I:ASP87 3.6 54.6 1.0 O3A I:AGS1 3.8 42.7 1.0 O3B I:AGS1 3.9 46.5 1.0 O2G I:AGS1 4.1 48.1 1.0 O I:HOH5495 4.1 46.7 1.0 O I:HOH5267 4.2 53.9 1.0 O I:HOH5261 4.3 63.0 1.0 C5' I:AGS1 4.4 41.3 1.0 O5' I:AGS1 4.5 40.8 1.0 N I:GLY88 4.5 44.1 1.0 O1A I:AGS1 4.7 37.7 1.0 CB I:ASP87 4.7 50.8 1.0 S1G I:AGS1 4.7 47.8 1.0 O2B I:AGS1 4.8 44.6 1.0 O I:HOH1499 4.9 47.9 1.0

Magnesium binding site 10 out of 14 in the Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 10 of Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ J:Mg550 b:37.0 occ:1.00 O J:HOH5451 2.2 64.1 1.0 O J:HOH5450 2.2 51.3 1.0 O3G J:AGS1 2.2 54.5 1.0 OD1 J:ASP87 2.3 55.3 1.0 O2A J:AGS1 2.3 43.3 1.0 O1B J:AGS1 2.4 51.5 1.0 CG J:ASP87 3.3 53.3 1.0 PB J:AGS1 3.5 47.8 1.0 OD2 J:ASP87 3.5 54.7 1.0 PG J:AGS1 3.5 55.0 1.0 PA J:AGS1 3.6 43.2 1.0 O3A J:AGS1 3.8 45.3 1.0 O3B J:AGS1 3.9 49.8 1.0 O2G J:AGS1 4.0 53.3 1.0 O J:HOH5499 4.1 44.2 1.0 O J:HOH5297 4.4 51.8 1.0 O J:HOH2699 4.4 68.8 1.0 N J:GLY88 4.4 46.5 1.0 O5' J:AGS1 4.5 41.5 1.0 C5' J:AGS1 4.5 40.7 1.0 CB J:ASP87 4.6 50.2 1.0 S1G J:AGS1 4.7 53.5 1.0 O1A J:AGS1 4.7 41.8 1.0 O2B J:AGS1 4.9 49.4 1.0 CA J:ASP87 5.0 50.0 1.0

J.Wang, D.C.Boisvert. Structural Basis For Groel-Assisted Protein Folding From the Crystal Structure of (Groel-Kmgatp)14 at 2.0 A Resolution J.Mol.Biol. V. 327 843 2003.
ISSN: ISSN 0022-2836
PubMed: 12654267
DOI: 10.1016/S0022-2836(03)00184-0