4Y72

Human CDK1/CyclinB1/CKS2 With Inhibitor


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.252 
  • R-Value Work: 0.186 
  • R-Value Observed: 0.190 

Starting Models: experimental
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wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

CDK1 structures reveal conserved and unique features of the essential cell cycle CDK.

Brown, N.R.Korolchuk, S.Martin, M.P.Stanley, W.A.Moukhametzianov, R.Noble, M.E.Endicott, J.A.

(2015) Nat Commun 6: 6769-6769

  • DOI: https://doi.org/10.1038/ncomms7769
  • Primary Citation of Related Structures:  
    4Y72, 4YC3, 4YC6, 5HQ0

  • PubMed Abstract: 

    CDK1 is the only essential cell cycle CDK in human cells and is required for successful completion of M-phase. It is the founding member of the CDK family and is conserved across all eukaryotes. Here we report the crystal structures of complexes of CDK1-Cks1 and CDK1-cyclin B-Cks2. These structures confirm the conserved nature of the inactive monomeric CDK fold and its ability to be remodelled by cyclin binding. Relative to CDK2-cyclin A, CDK1-cyclin B is less thermally stable, has a smaller interfacial surface, is more susceptible to activation segment dephosphorylation and shows differences in the substrate sequence features that determine activity. Both CDK1 and CDK2 are potential cancer targets for which selective compounds are required. We also describe the first structure of CDK1 bound to a potent ATP-competitive inhibitor and identify aspects of CDK1 structure and plasticity that might be exploited to develop CDK1-selective inhibitors.


  • Organizational Affiliation

    Department of Biochemistry, University of Oxford, South Parks Road, Oxford, Oxfordshire OX1 3QU, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Cyclin-dependent kinase 1302Homo sapiensMutation(s): 0 
Gene Names: CDK1CDC2CDC28ACDKN1P34CDC2
EC: 2.7.11.22 (PDB Primary Data), 2.7.11.23 (PDB Primary Data)
UniProt & NIH Common Fund Data Resources
Find proteins for P06493 (Homo sapiens)
Explore P06493 
Go to UniProtKB:  P06493
PHAROS:  P06493
GTEx:  ENSG00000170312 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP06493
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
G2/mitotic-specific cyclin-B1273Homo sapiensMutation(s): 0 
Gene Names: CCNB1CCNB
UniProt & NIH Common Fund Data Resources
Find proteins for P14635 (Homo sapiens)
Explore P14635 
Go to UniProtKB:  P14635
PHAROS:  P14635
GTEx:  ENSG00000134057 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP14635
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Cyclin-dependent kinases regulatory subunit 284Homo sapiensMutation(s): 0 
Gene Names: CKS2
UniProt & NIH Common Fund Data Resources
Find proteins for P33552 (Homo sapiens)
Explore P33552 
Go to UniProtKB:  P33552
PHAROS:  P33552
GTEx:  ENSG00000123975 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP33552
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
LZ9
Query on LZ9

Download Ideal Coordinates CCD File 
D [auth A]{[(2,6-difluorophenyl)carbonyl]amino}-N-(4-fluorophenyl)-1H-pyrazole-3-carboxamide
C17 H11 F3 N4 O2
BDRDBXXWQDFXEC-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.252 
  • R-Value Work: 0.186 
  • R-Value Observed: 0.190 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 65.166α = 90
b = 68.646β = 90
c = 166.771γ = 90
Software Package:
Software NamePurpose
XDSdata reduction
Aimlessdata scaling
PHASERphasing
REFMACrefinement

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-08-12
    Type: Initial release
  • Version 1.1: 2024-01-10
    Changes: Data collection, Database references, Refinement description