PDBsum entry 3tnw

Transferase/transferase inhibitor

PDB id: 3tnw

Contents

Protein chains

296 a.a.

257 a.a.

Ligands

F18 ×2

Metals

_NA ×2

Waters ×912

PDB id:

3tnw

Name:

Transferase/transferase inhibitor

Title:

Structure of cdk2/cyclin a in complex with can508

Structure:

Cyclin-dependent kinase 2. Chain: a, c. Synonym: cell division protein kinase 2, p33 protein kinase. Engineered: yes. Cyclin-a2. Chain: b, d. Fragment: cyclin boxes, unp resdiues 169-430. Synonym: cyclin-a. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: cdk2. Expressed in: escherichia coli. Expression_system_taxid: 562. Bos taurus. Bovine. Organism_taxid: 9913.

Resolution:

2.00Å R-factor: 0.188 R-free: 0.227

Authors:

S.Baumli,A.J.Hole,J.A.Endicott

Key ref:

S.Baumli et al. (2012). The CDK9 C-helix exhibits conformational plasticity that may explain the selectivity of CAN508. Acs Chem Biol, 7, 811-816. PubMed id: 22292676

Date:

02-Sep-11 Release date: 15-Feb-12

Protein chains

P24941  (CDK2_HUMAN) -  Cyclin-dependent kinase 2 from Homo sapiens

Seq: 298 a.a.

Struc: 296 a.a.*

Protein chains

P30274  (CCNA2_BOVIN) -  Cyclin-A2 from Bos taurus

Seq: 430 a.a.

Struc: 257 a.a.

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: Chains A, C: E.C.2.7.11.22 - cyclin-dependent 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

Acs Chem Biol 7:811-816 (2012)

PubMed id: 22292676

The CDK9 C-helix exhibits conformational plasticity that may explain the selectivity of CAN508.

S.Baumli, A.J.Hole, M.E.Noble, J.A.Endicott.

ABSTRACT

No abstract given.