PDBsum entry 5lvm

Transferase

PDB id: 5lvm

Contents

Protein chain

284 a.a.

Ligands

ADE

DTD

Waters ×314

PDB id:

5lvm

Name:

Transferase

Title:

Human pdk1 kinase domain in complex with adenine bound to the atp- binding site

Structure:

3-phosphoinositide-dependent protein kinase 1. Chain: a. Synonym: hpdk1. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: pdpk1, pdk1. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108

Resolution:

1.26Å R-factor: 0.135 R-free: 0.155

Authors:

J.O.Schulze,G.Saladino,K.Busschots,S.Neimanis,E.Suess,D.Odadzic, S.Zeuzem,V.Hindie,A.K.Herbrand,M.N.Lisa,P.M.Alzari,F.L.Gervasio, R.M.Biondi

Key ref:

J.O.Schulze et al. (2016). Bidirectional Allosteric Communication between the ATP-Binding Site and the Regulatory PIF Pocket in PDK1 Protein Kinase. Cell Chem Biol, 23, 1193-1205. PubMed id: 27693059 DOI: 10.1016/j.chembiol.2016.06.017

Date:

14-Sep-16 Release date: 19-Oct-16

Protein chain

O15530  (PDPK1_HUMAN) -  3-phosphoinositide-dependent protein kinase 1 from Homo sapiens

Seq: 556 a.a.

Struc: 284 a.a.*

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

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: 10.1016/j.chembiol.2016.06.017

Cell Chem Biol 23:1193-1205 (2016)

PubMed id: 27693059

Bidirectional Allosteric Communication between the ATP-Binding Site and the Regulatory PIF Pocket in PDK1 Protein Kinase.

J.O.Schulze, G.Saladino, K.Busschots, S.Neimanis, E.Süß, D.Odadzic, S.Zeuzem, V.Hindie, A.K.Herbrand, M.N.Lisa, P.M.Alzari, F.L.Gervasio, R.M.Biondi.

ABSTRACT

No abstract given.