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Magnesium in PDB 4nh1: Crystal Structure of A Heterotetrameric CK2 Holoenzyme Complex Carrying the Andante-Mutation in CK2BETA and Consistent with Proposed Models of Autoinhibition and Trans-Autophosphorylation

Enzymatic activity of Crystal Structure of A Heterotetrameric CK2 Holoenzyme Complex Carrying the Andante-Mutation in CK2BETA and Consistent with Proposed Models of Autoinhibition and Trans-Autophosphorylation

All present enzymatic activity of Crystal Structure of A Heterotetrameric CK2 Holoenzyme Complex Carrying the Andante-Mutation in CK2BETA and Consistent with Proposed Models of Autoinhibition and Trans-Autophosphorylation:
2.7.11.1;

Protein crystallography data

The structure of Crystal Structure of A Heterotetrameric CK2 Holoenzyme Complex Carrying the Andante-Mutation in CK2BETA and Consistent with Proposed Models of Autoinhibition and Trans-Autophosphorylation, PDB code: 4nh1 was solved by A.Schnitzler, O.-G.Issinger, K.Niefind, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.24 / 3.30
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 210.537, 57.441, 139.394, 90.00, 118.54, 90.00
R / Rfree (%) 21.3 / 25.1

Other elements in 4nh1:

The structure of Crystal Structure of A Heterotetrameric CK2 Holoenzyme Complex Carrying the Andante-Mutation in CK2BETA and Consistent with Proposed Models of Autoinhibition and Trans-Autophosphorylation also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of A Heterotetrameric CK2 Holoenzyme Complex Carrying the Andante-Mutation in CK2BETA and Consistent with Proposed Models of Autoinhibition and Trans-Autophosphorylation (pdb code 4nh1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of A Heterotetrameric CK2 Holoenzyme Complex Carrying the Andante-Mutation in CK2BETA and Consistent with Proposed Models of Autoinhibition and Trans-Autophosphorylation, PDB code: 4nh1:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 4nh1

Go back to Magnesium Binding Sites List in 4nh1
Magnesium binding site 1 out of 4 in the Crystal Structure of A Heterotetrameric CK2 Holoenzyme Complex Carrying the Andante-Mutation in CK2BETA and Consistent with Proposed Models of Autoinhibition and Trans-Autophosphorylation


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 Heterotetrameric CK2 Holoenzyme Complex Carrying the Andante-Mutation in CK2BETA and Consistent with Proposed Models of Autoinhibition and Trans-Autophosphorylation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:65.6
occ:0.44
 O3G A:ACP403 2.1 0.5 0.9
O A:HOH502 2.1 0.4 1.0
O2A A:ACP403 2.1 0.6 0.9
OD2 A:ASP175 2.1 0.4 1.0
OD1 A:ASN161 2.2 0.2 1.0
CG A:ASP175 3.1 0.7 1.0
CG A:ASN161 3.1 0.1 1.0
O1B A:ACP403 3.2 0.5 0.9
PG A:ACP403 3.4 0.6 0.9
ND2 A:ASN161 3.5 0.8 1.0
PA A:ACP403 3.6 0.4 0.9
MG A:MG402 3.6 0.2 1.0
CB A:ASP175 3.7 0.5 1.0
PB A:ACP403 3.7 0.1 0.9
C3B A:ACP403 3.8 0.1 0.9
O2G A:ACP403 3.9 0.3 0.9
O3A A:ACP403 3.9 78.0 0.9
OD1 A:ASP175 4.2 0.5 1.0
O A:HIS160 4.3 0.0 1.0
C5' A:ACP403 4.4 0.5 0.9
O5' A:ACP403 4.4 0.1 0.9
CB A:ASN161 4.5 95.0 1.0
O1A A:ACP403 4.5 97.2 0.9
O1G A:ACP403 4.6 1.0 0.9
OD2 A:ASP156 4.6 0.9 1.0
CA A:ASN161 5.0 96.5 1.0
C A:HIS160 5.0 0.5 1.0

Magnesium binding site 2 out of 4 in 4nh1

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Magnesium binding site 2 out of 4 in the Crystal Structure of A Heterotetrameric CK2 Holoenzyme Complex Carrying the Andante-Mutation in CK2BETA and Consistent with Proposed Models of Autoinhibition and Trans-Autophosphorylation


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 Heterotetrameric CK2 Holoenzyme Complex Carrying the Andante-Mutation in CK2BETA and Consistent with Proposed Models of Autoinhibition and Trans-Autophosphorylation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:0.2
occ:1.00
 O1B A:ACP403 2.0 0.5 0.9
OD1 A:ASP175 2.0 0.5 1.0
O2G A:ACP403 2.0 0.3 0.9
OD2 A:ASP175 2.1 0.4 1.0
CG A:ASP175 2.3 0.7 1.0
PB A:ACP403 3.2 0.1 0.9
PG A:ACP403 3.3 0.6 0.9
O3G A:ACP403 3.5 0.5 0.9
MG A:MG401 3.6 65.6 0.4
CB A:ASP175 3.8 0.5 1.0
OD2 A:ASP156 3.8 0.9 1.0
C3B A:ACP403 3.9 0.1 0.9
O2B A:ACP403 4.0 0.1 0.9
CD1 A:LEU178 4.0 0.5 1.0
O2A A:ACP403 4.2 0.6 0.9
O1G A:ACP403 4.5 1.0 0.9
O3A A:ACP403 4.5 78.0 0.9
CA A:ASP175 4.6 0.2 1.0
NZ A:LYS68 4.8 95.1 1.0
PA A:ACP403 4.8 0.4 0.9
C A:ASP175 4.9 0.8 1.0

Magnesium binding site 3 out of 4 in 4nh1

Go back to Magnesium Binding Sites List in 4nh1
Magnesium binding site 3 out of 4 in the Crystal Structure of A Heterotetrameric CK2 Holoenzyme Complex Carrying the Andante-Mutation in CK2BETA and Consistent with Proposed Models of Autoinhibition and Trans-Autophosphorylation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of A Heterotetrameric CK2 Holoenzyme Complex Carrying the Andante-Mutation in CK2BETA and Consistent with Proposed Models of Autoinhibition and Trans-Autophosphorylation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg401

b:0.5
occ:1.00
 O1B B:ACP404 2.0 0.1 1.0
OD1 B:ASP175 2.0 0.4 1.0
OD2 B:ASP175 2.0 0.1 1.0
O2G B:ACP404 2.0 0.8 1.0
O B:HOH505 2.1 99.7 1.0
CG B:ASP175 2.3 0.3 1.0
PB B:ACP404 3.2 0.5 1.0
PG B:ACP404 3.3 0.3 1.0
O3G B:ACP404 3.4 0.8 1.0
MG B:MG402 3.6 27.8 0.3
OD2 B:ASP156 3.6 0.3 1.0
CB B:ASP175 3.8 0.0 1.0
C3B B:ACP404 3.9 0.7 1.0
CD1 B:LEU178 4.0 0.4 1.0
O2B B:ACP404 4.1 0.6 1.0
O2A B:ACP404 4.1 0.2 1.0
O3A B:ACP404 4.5 0.4 1.0
O1G B:ACP404 4.5 0.3 1.0
CA B:ASP175 4.6 0.1 1.0
PA B:ACP404 4.8 0.5 1.0
CG B:ASP156 4.8 0.6 1.0
NZ B:LYS68 4.9 91.7 1.0
ND2 B:ASN161 4.9 1.0 1.0
O1A B:ACP404 4.9 0.0 1.0
C B:ASP175 4.9 0.5 1.0
OD1 B:ASN161 5.0 0.4 1.0

Magnesium binding site 4 out of 4 in 4nh1

Go back to Magnesium Binding Sites List in 4nh1
Magnesium binding site 4 out of 4 in the Crystal Structure of A Heterotetrameric CK2 Holoenzyme Complex Carrying the Andante-Mutation in CK2BETA and Consistent with Proposed Models of Autoinhibition and Trans-Autophosphorylation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of A Heterotetrameric CK2 Holoenzyme Complex Carrying the Andante-Mutation in CK2BETA and Consistent with Proposed Models of Autoinhibition and Trans-Autophosphorylation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg402

b:27.8
occ:0.29
 O3G B:ACP404 2.0 0.8 1.0
O2A B:ACP404 2.1 0.2 1.0
O B:HOH502 2.1 0.5 1.0
OD2 B:ASP175 2.1 0.1 1.0
OD1 B:ASN161 2.1 0.4 1.0
CG B:ASN161 3.1 0.1 1.0
CG B:ASP175 3.1 0.3 1.0
O1B B:ACP404 3.2 0.1 1.0
PG B:ACP404 3.4 0.3 1.0
ND2 B:ASN161 3.4 1.0 1.0
PA B:ACP404 3.5 0.5 1.0
MG B:MG401 3.6 0.5 1.0
CB B:ASP175 3.6 0.0 1.0
PB B:ACP404 3.7 0.5 1.0
C3B B:ACP404 3.8 0.7 1.0
O2G B:ACP404 3.8 0.8 1.0
O3A B:ACP404 3.9 0.4 1.0
OD1 B:ASP175 4.1 0.4 1.0
C5' B:ACP404 4.3 0.8 1.0
O B:HIS160 4.3 0.6 1.0
O5' B:ACP404 4.4 0.4 1.0
CB B:ASN161 4.5 79.3 1.0
O1A B:ACP404 4.5 0.0 1.0
O1G B:ACP404 4.6 0.3 1.0
OD2 B:ASP156 4.6 0.3 1.0
CA B:ASN161 4.9 90.9 1.0
C B:HIS160 5.0 0.5 1.0

Reference:

A.Schnitzler, B.B.Olsen, O.-G.Issinger, K.Niefind. The Protein Kinase CK2(Andante) Holoenzyme Structure Supports Proposed Models of Autoregulation and Trans-Autophosphorylation J.Mol.Biol. V. 426 1871 2014.
ISSN: ISSN 0022-2836
PubMed: 24594356
DOI: 10.1016/J.JMB.2014.02.018
Page generated: Mon Aug 11 20:43:21 2025

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