PDBsum entry 3uyt

Transferase/transferase inhibitor

PDB id: 3uyt

Contents

Protein chains

287 a.a.

268 a.a.

Ligands

0CK ×4

SO4 ×7

Waters ×940

PDB id:

3uyt

Name:

Transferase/transferase inhibitor

Title:

Crystal structure of ck1d with pf670462 from p1 crystal form

Structure:

Casein kinase i isoform delta. Chain: a, b, c, d. Synonym: cki-delta, ckid. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: csnk1d. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108

Resolution:

2.00Å R-factor: 0.244 R-free: 0.264

Authors:

X.Huang

Key ref:

A.Long et al. (2012). Structural basis for the interaction between casein kinase 1 delta and a potent and selective inhibitor. J Med Chem, 55, 956-960. PubMed id: 22168824

Date:

06-Dec-11 Release date: 11-Jan-12

Protein chains

P48730  (KC1D_HUMAN) -  Casein kinase I isoform delta from Homo sapiens

Seq: 415 a.a.

Struc: 287 a.a.

Protein chain

P48730  (KC1D_HUMAN) -  Casein kinase I isoform delta from Homo sapiens

Seq: 415 a.a.

Struc: 268 a.a.

Enzyme reactions

• Enzyme class 1: Chains A, B, C, D: 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⁺
• Enzyme class 2: Chains A, B, C, D: E.C.2.7.11.26 - [tau protein] kinase.
• Reaction:
  1. L-seryl-[tau protein] + ATP = O-phospho-L-seryl-[tau protein] + ADP + H⁺
  2. L-threonyl-[tau protein] + ATP = O-phospho-L-threonyl-[tau protein] + ADP + H⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

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

reference

J Med Chem 55:956-960 (2012)

PubMed id: 22168824

Structural basis for the interaction between casein kinase 1 delta and a potent and selective inhibitor.

A.Long, H.Zhao, X.Huang.

ABSTRACT

Casein kinase 1 delta (CK1δ) and its closest homologue CK1ε are key regulators of diverse cellular growth and survival processes such as Wnt signaling, DNA repair, and circadian rhythms. We report three crystal structures of the kinase domain of human CK1δ, one apo and two complexed with a potent and selective CK1δ/ε inhibitor PF670462 in two different crystal forms. These structures provide a molecular basis for the strong and specific inhibitor interactions and suggest clues for further development of CK1δ/ε inhibitors.