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Zinc 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:

Magnesium (Mg) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc 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 Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4nh1

Go back to Zinc Binding Sites List in 4nh1
Zinc binding site 1 out of 2 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 Zinc with other atoms in the Zn 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
C:Zn301

b:96.4
occ:1.00
 SG C:CYS137 2.2 0.3 1.0
SG C:CYS109 2.3 91.1 1.0
SG C:CYS114 2.3 88.3 1.0
SG C:CYS140 2.3 83.1 1.0
CB C:CYS137 2.9 82.1 1.0
CB C:CYS140 3.0 86.5 1.0
CB C:CYS109 3.2 83.9 1.0
CB C:CYS114 3.3 88.4 1.0
N C:CYS140 3.6 0.2 1.0
CA C:CYS140 3.9 0.5 1.0
OH C:TYR144 4.2 0.4 1.0
CE1 C:TYR144 4.3 84.7 1.0
CA C:CYS137 4.3 0.6 1.0
CB C:ARG111 4.4 85.8 1.0
NE C:ARG111 4.4 98.5 1.0
CB C:LYS139 4.6 91.5 1.0
CA C:CYS109 4.6 99.4 1.0
CZ C:TYR144 4.6 0.3 1.0
C C:LYS139 4.6 97.7 1.0
O C:CYS137 4.7 0.6 1.0
CA C:CYS114 4.7 0.3 1.0
C C:CYS137 4.7 0.3 1.0
CD C:ARG111 4.8 91.1 1.0
C C:CYS140 4.9 94.7 1.0
N C:LYS139 4.9 0.9 1.0
CA C:LYS139 5.0 96.0 1.0

Zinc binding site 2 out of 2 in 4nh1

Go back to Zinc Binding Sites List in 4nh1
Zinc binding site 2 out of 2 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 Zinc with other atoms in the Zn 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
D:Zn301

b:86.2
occ:1.00
 SG D:CYS137 2.3 0.3 1.0
SG D:CYS109 2.3 83.0 1.0
SG D:CYS114 2.3 83.7 1.0
SG D:CYS140 2.3 81.6 1.0
CB D:CYS137 2.9 83.4 1.0
CB D:CYS140 3.0 81.9 1.0
CB D:CYS109 3.2 84.4 1.0
CB D:CYS114 3.3 84.9 1.0
N D:CYS140 3.6 0.9 1.0
CA D:CYS140 3.9 99.5 1.0
OH D:TYR144 4.1 0.7 1.0
CE1 D:TYR144 4.3 94.4 1.0
CA D:CYS137 4.4 0.1 1.0
CB D:ARG111 4.5 82.3 1.0
CZ D:TYR144 4.6 0.9 1.0
NE D:ARG111 4.6 97.2 1.0
CB D:LYS139 4.6 86.6 1.0
C D:LYS139 4.7 94.3 1.0
CA D:CYS109 4.7 99.3 1.0
CA D:CYS114 4.7 0.4 1.0
O D:CYS137 4.8 0.6 1.0
C D:CYS137 4.8 0.3 1.0
C D:CYS140 4.9 89.0 1.0
CD D:ARG111 4.9 88.2 1.0
N D:LYS139 5.0 0.1 1.0
CA D:LYS139 5.0 89.1 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: Sun Oct 27 03:11:59 2024

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