PDBsum entry 5yf9

Transferase

PDB id: 5yf9

Contents

Protein chains

319 a.a.

Ligands

NIO ×2

SO4 ×8

Waters ×992

PDB id:

5yf9

Name:

Transferase

Title:

Crystal structure of ck2a2 form-2

Structure:

Casein kinase ii subunit alpha'. Chain: x, b. Fragment: unp residues 1-334. Synonym: ck ii alpha'. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: csnk2a2, ck2a2. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.89Å R-factor: 0.214 R-free: 0.263

Authors:

M.Tsuyuguchi,T.Kinoshita

Key ref:

M.Tsuyuguchi et al. (2018). Crystal structures of human CK2α2 in new crystal forms arising from a subtle difference in salt concentration. Acta Crystallogr F Struct Biol Commun, 74, 288-293. PubMed id: 29717996 DOI: 10.1107/S2053230X18005204

Date:

20-Sep-17 Release date: 16-May-18

Protein chains

P19784  (CSK22_HUMAN) -  Casein kinase II subunit alpha' from Homo sapiens

Seq: 350 a.a.

Struc: 319 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.11.1 - non-specific serine/threonine protein kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1107/S2053230X18005204

Acta Crystallogr F Struct Biol Commun 74:288-293 (2018)

PubMed id: 29717996

Crystal structures of human CK2α2 in new crystal forms arising from a subtle difference in salt concentration.

M.Tsuyuguchi, T.Nakaniwa, T.Kinoshita.

ABSTRACT

The catalytic subunits of protein kinase CK2 are classified into two subtypes: CK2α1 and CK2α2. CK2α1 is an attractive drug-discovery target for various diseases such as cancers and nephritis. CK2α2 is defined as an off-target of CK2α1 and is a potential target in the development of male contraceptive drugs. High-resolution crystal structures of both isozymes are likely to provide crucial clues for the design of selective inhibitors of CK2α1 and/or CK2α2. To date, several crystal structures of CK2α1 have been solved at high resolutions of beyond 1.5 Å. However, crystal structures of CK2α2 have barely achieved a low resolution of around 3 Å because of the formation of needle-shaped crystals. In this study, new crystal forms were exploited and one provided a crystal structure of CK2α2 at 1.89 Å resolution. This result, together with the structure of CK2α1, will assist in the development of highly selective inhibitors for both isozymes.