PDBsum entry 3tnh

Transferase/transferase inhibitor

PDB id: 3tnh

Contents

Protein chains

289 a.a.

244 a.a.

Ligands

F18

PDB id:

3tnh

Name:

Transferase/transferase inhibitor

Title:

Cdk9/cyclin t in complex with can508

Structure:

Cyclin-dependent kinase 9. Chain: a. Fragment: kinase domain, unp residues 2-330. Synonym: c-2k, cell division cycle 2-like protein kinase 4, cell division protein kinase 9, serine/threonine-protein kinase pitalre. Engineered: yes. Cyclin-t1. Chain: b. Fragment: cyclin boxes, unp residues 1-259.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: cdc2l4, cdk9. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9. Gene: ccnt1.

Resolution:

3.20Å R-factor: 0.179 R-free: 0.226

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:

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

Protein chain

P50750  (CDK9_HUMAN) -  Cyclin-dependent kinase 9 from Homo sapiens

Seq: 372 a.a.

Struc: 289 a.a.*

Protein chain

O60563  (CCNT1_HUMAN) -  Cyclin-T1 from Homo sapiens

Seq: 726 a.a.

Struc: 244 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class 2: Chain A: 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⁺
• Enzyme class 3: Chain A: E.C.2.7.11.23 - [RNA-polymerase]-subunit kinase.
• Reaction: [DNA-directed RNA polymerase] + ATP = phospho-[DNA-directed RNA polymerase] + 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

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.