Atomistry » Magnesium » PDB 1zk3-207d » 1zy5
Atomistry »
  Magnesium »
    PDB 1zk3-207d »
      1zy5 »

Magnesium in PDB 1zy5: Crystal Structure of EIF2ALPHA Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with Amppnp.

Enzymatic activity of Crystal Structure of EIF2ALPHA Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with Amppnp.

All present enzymatic activity of Crystal Structure of EIF2ALPHA Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with Amppnp.:
2.7.1.37;

Protein crystallography data

The structure of Crystal Structure of EIF2ALPHA Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with Amppnp., PDB code: 1zy5 was solved by A.K.Padyana, H.Qiu, A.Roll-Mecak, A.G.Hinnebusch, S.K.Burley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.58 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.610, 78.919, 146.299, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of EIF2ALPHA Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with Amppnp. (pdb code 1zy5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of EIF2ALPHA Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with Amppnp., PDB code: 1zy5:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1zy5

Go back to Magnesium Binding Sites List in 1zy5
Magnesium binding site 1 out of 2 in the Crystal Structure of EIF2ALPHA Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with Amppnp.


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 EIF2ALPHA Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with Amppnp. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg305

b:98.3
occ:1.00
O1A A:ANP303 2.0 64.9 1.0
O2G A:ANP303 2.2 94.9 1.0
O A:HOH205 2.3 73.4 1.0
O3G A:ANP303 2.8 92.9 1.0
PG A:ANP303 3.0 97.1 1.0
NZ A:LYS628 3.3 52.1 1.0
PA A:ANP303 3.4 72.9 1.0
O2A A:ANP303 3.9 63.1 1.0
N3B A:ANP303 4.0 80.0 1.0
O A:HOH114 4.0 41.0 1.0
O1G A:ANP303 4.1 90.3 1.0
OD2 A:ASP853 4.2 37.9 1.0
O1B A:ANP303 4.2 78.1 1.0
O3A A:ANP303 4.3 63.1 1.0
O5' A:ANP303 4.4 59.0 1.0
PB A:ANP303 4.4 71.8 1.0
CE A:LYS628 4.7 44.9 1.0
O A:HOH138 4.7 56.1 1.0
O A:HOH90 4.7 50.1 1.0
C5' A:ANP303 4.8 48.7 1.0
CG A:ASP853 4.9 48.2 1.0
OD1 A:ASP853 4.9 60.1 1.0

Magnesium binding site 2 out of 2 in 1zy5

Go back to Magnesium Binding Sites List in 1zy5
Magnesium binding site 2 out of 2 in the Crystal Structure of EIF2ALPHA Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with Amppnp.


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 EIF2ALPHA Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with Amppnp. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg306

b:94.7
occ:1.00
O1B B:ANP304 2.0 89.1 1.0
O2G B:ANP304 2.0 0.4 1.0
PB B:ANP304 3.3 0.7 1.0
PG B:ANP304 3.3 0.7 1.0
O1A B:ANP304 3.3 86.3 1.0
N3B B:ANP304 3.7 0.6 1.0
CZ B:PHE610 3.8 0.1 1.0
O3A B:ANP304 4.0 97.5 1.0
PA B:ANP304 4.1 84.5 1.0
O B:HOH201 4.3 70.7 1.0
O3G B:ANP304 4.3 0.1 1.0
O1G B:ANP304 4.3 0.1 1.0
O2B B:ANP304 4.4 1.0 1.0
CE2 B:PHE610 4.4 0.0 1.0
O2A B:ANP304 4.4 87.3 1.0
CE1 B:PHE610 4.7 0.6 1.0
CA B:GLY608 4.7 71.4 1.0
O B:GLN607 4.7 73.4 1.0

Reference:

A.K.Padyana, H.Qiu, A.Roll-Mecak, A.G.Hinnebusch, S.K.Burley. Structural Basis For Autoinhibition and Mutational Activation of Eukaryotic Initiation Factor 2{Alpha} Protein Kinase GCN2 J.Biol.Chem. V. 280 29289 2005.
ISSN: ISSN 0021-9258
PubMed: 15964839
DOI: 10.1074/JBC.M504096200
Page generated: Tue Aug 13 20:16:12 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy