Brand  (β version)

PDB ID: 4OTH

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Ligands
Code Name Style Show Link
DRN Bisindolylmaleimide ix PoSSuM
Non-standard Residues
Code Name Show
SEP Phosphoserine
TPO Phosphothreonine
Glycosylation
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Structure summary

Code : 4OTH   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE/TRANSFERASE INHIBITOR
Title : Crystal Structure of PRK1 Catalytic Domain in Complex with Ro-31-8220
Release Data : 2014-08-27
Compound :
mol_id molecule chains synonym
1 Serine/threonine-protein kinase N1 A Protease-activated kinase 1, PAK-1, Protein kinase C-like 1, Protein kinase C-like PKN, Protein kinase PKN-alpha, Protein-kinase C-related kinase 1, Serine-threonine protein kinase N
ec: 2.7.11.13
fragment: UNP residues 605-942
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Trichoplusia ni  (taxid:7111)
gene: PKN1, PAK1, PKN, PRK1, PRKCL1
Authors : Chamberlain, P.P., Delker, S., Pagarigan, B., Mahmoudi, A., Jackson, P., Abbassian, M., Muir, J., Raheja, N., Cathers, B.
Keywords : PRK1, PKN1, Protein kinase C related kinase 1, KINASE, PROTEIN KINASE, ATP BINDING, PHOSPHORYLATION, TRANSFERASE-TRANSFERASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 1.8000 Å )
Citation :

Crystal Structures of PRK1 in Complex with the Clinical Compounds Lestaurtinib and Tofacitinib Reveal Ligand Induced Conformational Changes.

Chamberlain, P.,Delker, S.,Pagarigan, B.  et al.
(2014)  Plos One  9 : e103638 - e103638

PubMed: 25111382
DOI: 10.1371/journal.pone.0103638

Reaction

Chain : A
UniProt : Q16512 (PKN1_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein] 2.7.11.13 PubMed:18066052
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ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein] 2.7.11.13 PubMed:18066052
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