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Chlorine in PDB 9hk5: Structure of A Mutant of Human Protein Kinase CK2ALPHA' That Equals Its Isoenzyme CK2ALPHA in Affinity to the Regulatory Subunit CK2BETA

Enzymatic activity of Structure of A Mutant of Human Protein Kinase CK2ALPHA' That Equals Its Isoenzyme CK2ALPHA in Affinity to the Regulatory Subunit CK2BETA

All present enzymatic activity of Structure of A Mutant of Human Protein Kinase CK2ALPHA' That Equals Its Isoenzyme CK2ALPHA in Affinity to the Regulatory Subunit CK2BETA:
2.7.11.1;

Protein crystallography data

The structure of Structure of A Mutant of Human Protein Kinase CK2ALPHA' That Equals Its Isoenzyme CK2ALPHA in Affinity to the Regulatory Subunit CK2BETA, PDB code: 9hk5 was solved by C.Werner, K.Niefind, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.97 / 1.49
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 46.788, 47.804, 50.579, 111.76, 90.22, 91.55
R / Rfree (%) 17.4 / 20.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of A Mutant of Human Protein Kinase CK2ALPHA' That Equals Its Isoenzyme CK2ALPHA in Affinity to the Regulatory Subunit CK2BETA (pdb code 9hk5). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structure of A Mutant of Human Protein Kinase CK2ALPHA' That Equals Its Isoenzyme CK2ALPHA in Affinity to the Regulatory Subunit CK2BETA, PDB code: 9hk5:

Chlorine binding site 1 out of 1 in 9hk5

Go back to Chlorine Binding Sites List in 9hk5
Chlorine binding site 1 out of 1 in the Structure of A Mutant of Human Protein Kinase CK2ALPHA' That Equals Its Isoenzyme CK2ALPHA in Affinity to the Regulatory Subunit CK2BETA


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of A Mutant of Human Protein Kinase CK2ALPHA' That Equals Its Isoenzyme CK2ALPHA in Affinity to the Regulatory Subunit CK2BETA within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl402

b:45.6
occ:1.00
 CL22 A:3NG402 0.0 45.6 1.0
C18 A:3NG402 1.7 42.1 1.0
C17 A:3NG402 2.7 28.1 1.0
C19 A:3NG402 2.7 31.8 1.0
O A:HOH782 3.0 33.3 1.0
O A:HOH583 3.2 36.8 1.0
C A:GLY47 3.5 25.4 1.0
N A:ARG48 3.6 20.0 1.0
CA A:GLY47 3.6 26.8 1.0
O A:HOH543 3.7 30.0 1.0
CG2 A:VAL54 3.8 19.6 1.0
CB A:VAL54 4.0 13.6 1.0
C20 A:3NG402 4.0 36.8 1.0
C16 A:3NG402 4.0 21.3 1.0
O A:GLY47 4.1 18.4 1.0
N A:GLY47 4.2 19.3 1.0
NE2 A:HIS161 4.4 38.2 1.0
CA A:ARG48 4.4 23.0 1.0
C A:ARG48 4.4 35.8 1.0
O A:HOH524 4.5 15.4 1.0
C21 A:3NG402 4.5 30.5 1.0
O A:ARG48 4.6 37.1 1.0
CE1 A:HIS161 4.7 39.9 1.0
CG1 A:VAL54 4.8 16.0 1.0
N A:GLY49 4.8 42.8 1.0
C A:LEU46 4.8 22.5 1.0
O A:HOH738 5.0 33.7 1.0
N A:VAL54 5.0 10.8 1.0

Reference:

C.Werner, S.Eimermacher, H.Harasimowicz, D.Fischer, M.Pietsch, K.Niefind. A CK2 Alpha ' Mutant Indicating Why CK2 Alpha and CK2 Alpha ', the Isoforms of the Catalytic Subunit of Human Protein Kinase CK2, Deviate in Affinity to CK2 Beta. Biol.Chem. 2025.
ISSN: ISSN 1431-6730
PubMed: 40223482
DOI: 10.1515/HSZ-2024-0157
Page generated: Sun Jul 13 17:02:13 2025

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