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Magnesium in PDB 1lp4: Crystal Structure of A Binary Complex of the Catalytic Subunit of Protein Kinase CK2 with Mg-Amppnp

Enzymatic activity of Crystal Structure of A Binary Complex of the Catalytic Subunit of Protein Kinase CK2 with Mg-Amppnp

All present enzymatic activity of Crystal Structure of A Binary Complex of the Catalytic Subunit of Protein Kinase CK2 with Mg-Amppnp:
2.7.1.37;

Protein crystallography data

The structure of Crystal Structure of A Binary Complex of the Catalytic Subunit of Protein Kinase CK2 with Mg-Amppnp, PDB code: 1lp4 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) 55.00 / 1.86
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 144.075, 59.624, 45.642, 90.00, 103.59, 90.00
R / Rfree (%) 20.6 / 24.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of A Binary Complex of the Catalytic Subunit of Protein Kinase CK2 with Mg-Amppnp (pdb code 1lp4). 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 the Catalytic Subunit of Protein Kinase CK2 with Mg-Amppnp, PDB code: 1lp4:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1lp4

Go back to Magnesium Binding Sites List in 1lp4
Magnesium binding site 1 out of 2 in the Crystal Structure of A Binary Complex of the Catalytic Subunit of Protein Kinase CK2 with 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 the Catalytic Subunit of Protein Kinase CK2 with Mg-Amppnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg341

b:26.3
occ:1.00
O A:HOH627 2.1 22.7 1.0
O3G A:ANP340 2.1 23.6 1.0
OD1 A:ASP175 2.1 21.7 1.0
O A:HOH589 2.1 24.1 1.0
OD2 A:ASP175 2.2 21.3 1.0
O2B A:ANP340 2.2 22.9 1.0
CG A:ASP175 2.5 21.4 1.0
PG A:ANP340 3.2 26.3 1.0
PB A:ANP340 3.3 23.3 1.0
O1G A:ANP340 3.6 25.6 1.0
N3B A:ANP340 3.6 25.9 1.0
MG A:MG342 3.9 26.2 1.0
CB A:ASP175 4.0 20.2 1.0
OD2 A:ASP156 4.0 24.8 1.0
O A:HOH344 4.0 22.4 1.0
O1B A:ANP340 4.4 23.5 1.0
NZ A:LYS68 4.4 21.0 1.0
O A:HOH406 4.4 42.4 1.0
O2A A:ANP340 4.4 21.8 1.0
CA A:GLY177 4.4 25.4 1.0
O3A A:ANP340 4.5 22.8 1.0
N A:GLY177 4.5 24.7 1.0
O2G A:ANP340 4.6 24.3 1.0
O A:ASP175 4.7 20.6 1.0
CA A:ASP175 4.7 20.4 1.0
C A:GLY177 4.8 25.9 1.0
N A:LEU178 4.8 25.6 1.0
C A:ASP175 4.8 20.9 1.0
O A:HOH468 4.8 45.5 1.0
PA A:ANP340 4.9 22.9 1.0
ND2 A:ASN161 4.9 21.2 1.0
O1A A:ANP340 5.0 24.2 1.0
O A:HOH529 5.0 29.8 1.0

Magnesium binding site 2 out of 2 in 1lp4

Go back to Magnesium Binding Sites List in 1lp4
Magnesium binding site 2 out of 2 in the Crystal Structure of A Binary Complex of the Catalytic Subunit of Protein Kinase CK2 with 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 the Catalytic Subunit of Protein Kinase CK2 with Mg-Amppnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg342

b:26.2
occ:1.00
OD1 A:ASN161 2.1 20.3 1.0
O1G A:ANP340 2.1 25.6 1.0
O A:HOH628 2.1 23.7 1.0
O2A A:ANP340 2.1 21.8 1.0
OD2 A:ASP175 2.1 21.3 1.0
N3B A:ANP340 3.0 25.9 1.0
CG A:ASN161 3.0 21.4 1.0
CG A:ASP175 3.0 21.4 1.0
PG A:ANP340 3.1 26.3 1.0
ND2 A:ASN161 3.4 21.2 1.0
PA A:ANP340 3.5 22.9 1.0
CB A:ASP175 3.5 20.2 1.0
O3G A:ANP340 3.7 23.6 1.0
PB A:ANP340 3.8 23.3 1.0
MG A:MG341 3.9 26.3 1.0
O2B A:ANP340 3.9 22.9 1.0
O3A A:ANP340 3.9 22.8 1.0
CE A:LYS158 4.0 22.7 1.0
NZ A:LYS158 4.0 25.6 1.0
OD1 A:ASP175 4.1 21.7 1.0
O2G A:ANP340 4.3 24.3 1.0
O3' A:ANP340 4.3 23.2 1.0
O5' A:ANP340 4.3 22.8 1.0
C5' A:ANP340 4.4 20.4 1.0
CB A:ASN161 4.4 20.2 1.0
O1A A:ANP340 4.4 24.2 1.0
O A:HIS160 4.5 23.2 1.0
OD2 A:ASP156 4.5 24.8 1.0
CA A:ASN161 4.7 20.6 1.0
C3' A:ANP340 4.8 24.7 1.0
C A:HIS160 4.8 23.3 1.0
N A:ASN161 4.9 22.1 1.0
CA A:ASP175 4.9 20.4 1.0
O A:HOH589 5.0 24.1 1.0

Reference:

C.W.Yde, I.Ermakova, O.G.Issinger, K.Niefind. Inclining the Purine Base Binding Plane in Protein Kinase CK2 By Exchanging the Flanking Side-Chains Generates A Preference For Atp As A Cosubstrate. J.Mol.Biol. V. 347 399 2005.
ISSN: ISSN 0022-2836
PubMed: 15740749
DOI: 10.1016/J.JMB.2005.01.003
Page generated: Mon Dec 14 06:23:37 2020

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