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Magnesium in PDB 1tc0: Ligand Induced Conformational Shifts in the N-Terminal Domain of GRP94, Open Conformation Complexed with the Physiological Partner Atp

Protein crystallography data

The structure of Ligand Induced Conformational Shifts in the N-Terminal Domain of GRP94, Open Conformation Complexed with the Physiological Partner Atp, PDB code: 1tc0 was solved by D.T.Gewirth, R.M.Immormino, D.E.Dollins, P.L.Shaffer, M.A.Walker, K.L.Soldano, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.20
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 159.013, 159.013, 109.472, 90.00, 90.00, 120.00
R / Rfree (%) 22.6 / 26.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Ligand Induced Conformational Shifts in the N-Terminal Domain of GRP94, Open Conformation Complexed with the Physiological Partner Atp (pdb code 1tc0). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Ligand Induced Conformational Shifts in the N-Terminal Domain of GRP94, Open Conformation Complexed with the Physiological Partner Atp, PDB code: 1tc0:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1tc0

Go back to Magnesium Binding Sites List in 1tc0
Magnesium binding site 1 out of 2 in the Ligand Induced Conformational Shifts in the N-Terminal Domain of GRP94, Open Conformation Complexed with the Physiological Partner Atp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Ligand Induced Conformational Shifts in the N-Terminal Domain of GRP94, Open Conformation Complexed with the Physiological Partner Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:45.6
occ:1.00
O A:HOH526 2.2 37.6 1.0
O2A A:ATP301 2.2 28.3 1.0
O1B A:ATP301 2.3 42.7 1.0
ND2 A:ASN107 2.3 29.0 1.0
O A:HOH581 2.3 36.5 1.0
O A:HOH536 2.3 34.3 1.0
PB A:ATP301 3.3 40.4 1.0
CG A:ASN107 3.3 34.3 1.0
PA A:ATP301 3.5 32.6 1.0
OD1 A:ASN107 3.7 34.8 1.0
O3A A:ATP301 3.7 37.8 1.0
O3B A:ATP301 3.8 46.1 1.0
O A:HOH565 4.0 57.4 1.0
CA A:GLY198 4.1 43.8 1.0
O A:HOH514 4.2 27.1 1.0
OE1 A:GLU103 4.3 36.0 1.0
O5' A:ATP301 4.3 33.0 1.0
OG A:SER106 4.4 41.7 1.0
O A:HOH557 4.4 46.2 1.0
O A:GLU103 4.5 32.9 1.0
O1A A:ATP301 4.6 38.9 1.0
CB A:ASN107 4.6 33.3 1.0
OD1 A:ASP110 4.7 34.3 1.0
O2B A:ATP301 4.7 39.0 1.0
N A:ASN107 4.8 35.8 1.0
CA A:ASN107 4.8 33.5 1.0
N A:GLY198 4.8 45.0 1.0
C A:GLY198 4.8 43.8 1.0
N A:PHE199 4.9 42.4 1.0
CB A:SER106 4.9 35.2 1.0

Magnesium binding site 2 out of 2 in 1tc0

Go back to Magnesium Binding Sites List in 1tc0
Magnesium binding site 2 out of 2 in the Ligand Induced Conformational Shifts in the N-Terminal Domain of GRP94, Open Conformation Complexed with the Physiological Partner Atp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Ligand Induced Conformational Shifts in the N-Terminal Domain of GRP94, Open Conformation Complexed with the Physiological Partner Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg702

b:58.7
occ:1.00
O B:HOH844 2.3 39.5 1.0
O B:HOH829 2.3 44.7 1.0
O2A B:ATP601 2.3 38.9 1.0
O1B B:ATP601 2.3 43.2 1.0
OD1 B:ASN107 2.5 47.0 1.0
O B:HOH845 2.5 71.4 1.0
PB B:ATP601 3.2 46.9 1.0
CG B:ASN107 3.5 46.3 1.0
PA B:ATP601 3.5 42.3 1.0
O3A B:ATP601 3.6 44.8 1.0
O3B B:ATP601 3.6 48.7 1.0
O B:HOH859 3.6 54.5 1.0
ND2 B:ASN107 3.9 43.4 1.0
NZ A:LYS95 4.2 75.2 1.0
OE1 B:GLU103 4.2 53.0 1.0
OG B:SER106 4.2 48.5 1.0
CA B:GLY198 4.3 52.6 1.0
O B:HOH815 4.3 37.3 1.0
O5' B:ATP601 4.4 40.3 1.0
O B:GLU103 4.6 46.4 1.0
O1A B:ATP601 4.7 40.7 1.0
O2B B:ATP601 4.7 47.9 1.0
N B:GLY198 4.7 52.8 1.0
CB B:ASN107 4.8 43.8 1.0
N B:ASN107 4.8 44.4 1.0
CB B:SER106 4.8 44.2 1.0
OD1 B:ASP110 4.9 44.2 1.0
CA B:ASN107 4.9 44.4 1.0
C B:GLY198 5.0 51.6 1.0

Reference:

R.M.Immormino, D.E.Dollins, P.L.Shaffer, K.L.Soldano, M.A.Walker, D.T.Gewirth. Ligand-Induced Conformational Shift in the N-Terminal Domain of GRP94, An HSP90 Chaperone. J.Biol.Chem. V. 279 46162 2004.
ISSN: ISSN 0021-9258
PubMed: 15292259
DOI: 10.1074/JBC.M405253200
Page generated: Tue Aug 13 14:31:26 2024

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