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Magnesium in PDB 1daw: Crystal Structure of A Binary Complex of Protein Kinase CK2 (Alpha-Subunit) and Mg-Amppnp

Enzymatic activity of Crystal Structure of A Binary Complex of Protein Kinase CK2 (Alpha-Subunit) and Mg-Amppnp

All present enzymatic activity of Crystal Structure of A Binary Complex of Protein Kinase CK2 (Alpha-Subunit) and Mg-Amppnp:
2.7.1.37;

Protein crystallography data

The structure of Crystal Structure of A Binary Complex of Protein Kinase CK2 (Alpha-Subunit) and Mg-Amppnp, PDB code: 1daw was solved by K.Niefind, M.Puetter, B.Guerra, O.G.Issinger, D.Schomburg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 69.00 / 2.20
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 143.110, 59.200, 45.810, 90.00, 103.56, 90.00
R / Rfree (%) 21.2 / 28.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of A Binary Complex of Protein Kinase CK2 (Alpha-Subunit) and Mg-Amppnp (pdb code 1daw). 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 A Binary Complex of Protein Kinase CK2 (Alpha-Subunit) and Mg-Amppnp, PDB code: 1daw:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1daw

Go back to Magnesium Binding Sites List in 1daw
Magnesium binding site 1 out of 2 in the Crystal Structure of A Binary Complex of Protein Kinase CK2 (Alpha-Subunit) and Mg-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 A Binary Complex of Protein Kinase CK2 (Alpha-Subunit) and Mg-Amppnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg341

b:39.1
occ:1.00
O3G A:ANP340 2.0 30.9 1.0
O A:HOH354 2.1 34.6 1.0
O A:HOH520 2.3 29.8 1.0
OD2 A:ASP175 2.3 19.4 1.0
OD1 A:ASP175 2.4 19.8 1.0
O2B A:ANP340 2.4 36.0 1.0
CG A:ASP175 2.7 20.5 1.0
PG A:ANP340 2.8 34.2 1.0
PB A:ANP340 3.0 34.3 1.0
N3B A:ANP340 3.1 33.9 1.0
O1G A:ANP340 3.4 33.7 1.0
O3A A:ANP340 3.6 36.0 1.0
MG A:MG342 3.7 26.7 1.0
OD2 A:ASP156 3.9 27.9 1.0
O A:HOH368 4.0 28.7 1.0
O A:HOH409 4.2 41.0 1.0
O2G A:ANP340 4.2 32.7 1.0
CB A:ASP175 4.2 20.7 1.0
O1B A:ANP340 4.4 36.1 1.0
CD1 A:TYR50 4.4 55.8 1.0
O A:HOH578 4.5 64.3 1.0
NZ A:LYS68 4.5 28.9 1.0
O2A A:ANP340 4.6 32.4 1.0
CA A:GLY177 4.6 28.7 1.0
PA A:ANP340 4.7 32.2 1.0
N A:GLY177 4.8 25.3 1.0
ND2 A:ASN161 5.0 19.9 1.0

Magnesium binding site 2 out of 2 in 1daw

Go back to Magnesium Binding Sites List in 1daw
Magnesium binding site 2 out of 2 in the Crystal Structure of A Binary Complex of Protein Kinase CK2 (Alpha-Subunit) and Mg-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 A Binary Complex of Protein Kinase CK2 (Alpha-Subunit) and Mg-Amppnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg342

b:26.7
occ:1.00
O2A A:ANP340 1.8 32.4 1.0
OD2 A:ASP175 1.8 19.4 1.0
O A:HOH355 1.9 28.0 1.0
O1G A:ANP340 1.9 33.7 1.0
OD1 A:ASN161 2.1 19.3 1.0
O3A A:ANP340 2.7 36.0 1.0
PG A:ANP340 2.8 34.2 1.0
CG A:ASP175 2.9 20.5 1.0
PA A:ANP340 2.9 32.2 1.0
N3B A:ANP340 3.0 33.9 1.0
CG A:ASN161 3.2 21.7 1.0
CB A:ASP175 3.4 20.7 1.0
PB A:ANP340 3.5 34.3 1.0
ND2 A:ASN161 3.6 19.9 1.0
MG A:MG341 3.7 39.1 1.0
O3G A:ANP340 3.7 30.9 1.0
OD1 A:ASP175 3.9 19.8 1.0
O5' A:ANP340 3.9 32.8 1.0
C5' A:ANP340 4.0 30.0 1.0
O1A A:ANP340 4.1 31.9 1.0
O2G A:ANP340 4.1 32.7 1.0
O3' A:ANP340 4.2 28.8 1.0
CE A:LYS158 4.3 28.6 1.0
O2B A:ANP340 4.3 36.0 1.0
NZ A:LYS158 4.5 29.1 1.0
CB A:ASN161 4.5 21.3 1.0
OD2 A:ASP156 4.5 27.9 1.0
O A:HIS160 4.6 26.8 1.0
C3' A:ANP340 4.6 29.1 1.0
O A:HOH520 4.7 29.8 1.0
O1B A:ANP340 4.7 36.1 1.0
CA A:ASN161 4.8 22.6 1.0
CA A:ASP175 4.9 21.2 1.0
C4' A:ANP340 4.9 29.6 1.0
CD1 A:ILE174 5.0 24.3 1.0
C A:HIS160 5.0 28.4 1.0

Reference:

K.Niefind, M.Putter, B.Guerra, O.G.Issinger, D.Schomburg. Gtp Plus Water Mimic Atp in the Active Site of Protein Kinase CK2. Nat.Struct.Biol. V. 6 1100 1999.
ISSN: ISSN 1072-8368
PubMed: 10581548
DOI: 10.1038/70033
Page generated: Mon Dec 14 05:50:16 2020

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