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STRUCTURE OF HDAC4 CATALYTIC DOMAIN BOUND TO A HYDROXAMIC ACID INHBITOR
2VQM
Primary Citation
 
 
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  •   Molecular Description Hide
    Classification: Hydrolase
    Structure Weight: 45055.17
    Molecule: HISTONE DEACETYLASE 4
    Polymer: 1 Type: protein Length: 413
    Chains: A
    EC#: 3.5.1.98   
    Fragment: CATALYTIC DOMAIN, RESIDUES 648-1057
    Organism Homo sapiens
    Gene Names HDAC4 KIAA0288
    UniProtKB:   Protein Feature View | Search PDB | P56524  
     
  •   Source Hide
    Polymer: 1
    Scientific Name: Homo sapiens   Taxonomy   Common Name: Human Expression System: Escherichia coli  
     
  •   Related PDB Entries Hide
    Identifier Details
    2VQJ  STRUCTURE OF HDAC4 CATALYTIC DOMAIN BOUND TO A TRIFLUOROMETHYLKETONE INHBITOR 
    2VQO  STRUCTURE OF HDAC4 CATALYTIC DOMAIN WITH A GAIN-OF-FUNCTION MUATION BOUND TO A TRIFLUOROMETHYLKETONE INHBITOR 
    2VQQ  STRUCTURE OF HDAC4 CATALYTIC DOMAIN (A DOUBLE CYSTEINE-TO-ALANINE MUTANT) BOUND TO A TRIFLUOROMETHYLKETONE INHBITOR 
    2VQV  STRUCTURE OF HDAC4 CATALYTIC DOMAIN WITH A GAIN-OF-FUNCTION MUATION BOUND TO A HYDROXAMIC ACID INHIBITOR 
    2VQW  STRUCTURE OF INHIBITOR-FREE HDAC4 CATALYTIC DOMAIN (WITH GAIN-OF-FUNCTION MUTATION HIS332TYR) 
     
  •   Ligand Chemical Component Hide
    Identifier Formula Name Interactions
    HA3
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    Download      		HA3 C18 H16 N4 O3 S
    N-hydroxy-5-[(3-phenyl-5,6-dihydroimidazo[1,2- a]pyrazin-7(8H)-yl)carbonyl]thiophene-2-carboxamide
    		HA3:2VQM
    K
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    Download      		K K
    POTASSIUM ION
    ZN
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    Download      		ZN Zn
    ZINC ION
     
  •   External Ligand Annotations Hide
    Identifier   Binding Affinity (Sequence Identity %)
    HA3
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    Download      		HA3
    N/Ain BindingDB
    IC50: 975 nM - data from BindingMOAD  
    IC50: 978 nM - data from PDBbind  
     
  •   External Domain Annotations Hide
     
  •   Structural Biology Knowledgebase Data Hide
     
 
Data in orange boxes are gathered from external resources (when available).
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  Biological Assembly       
Biological assembly 1 assigned by authors and generated by PQS (software)
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