Brand  (β version)

PDB ID: 2VQM

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Ligands
Code Name Style Show Link
HA3 N-hydroxy-5-[(3-phenyl-5,6-dihydroimidazo[1,2-a]pyrazin-7(8h)-yl)carbonyl]thiophene-2-carboxamide PoSSuM
K Potassium ion PoSSuM
ZN Zinc ion PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 2VQM   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Structure of HDAC4 catalytic domain bound to a hydroxamic acid inhbitor
Release Data : 2008-07-08
Compound :
mol_id molecule chains synonym
1 HISTONE DEACETYLASE 4 A HD4
fragment: CATALYTIC DOMAIN, RESIDUES 648-1057
Source :
mol_id organism_scientific organism_common expression_system
1 HOMO SAPIENS  (taxid:9606) HUMAN ESCHERICHIA COLI  (taxid:469008)
expression_system_strain: BL21(DE3)
expression_system_plasmid: PETM-11 (OBTAINED FROM EMBL-HEIDELBERG)
Authors : Bottomley, M.J., Lo Surdo, P., Di Giovine, P., Cirillo, A., Scarpelli, R., Ferrigno, F., Jones, P., Neddermann, P., De Francesco, R., Steinkuhler, C., Gallinari, P., Carfi, A.
Keywords : INHIBITOR, REPRESSOR, CHROMATIN, COILED COIL, HISTONE DEACETYLASE, TRANSCRIPTION REGULATION, UBL CONJUGATION, CHROMATIN REGULATOR, POLYMORPHISM, TRANSCRIPTION, PHOSPHOPROTEIN, HDAC, ZINC, HDACI, NUCLEUS, HYDROLASE, CYTOPLASM
Exp. method : X-RAY DIFFRACTION ( 1.80 Å )
Citation :

Structural and Functional Analysis of the Human Hdac4 Catalytic Domain Reveals a Regulatory Zinc-Binding Domain.

Bottomley, M.J.,Lo Surdo, P.,Di Giovine, P.  et al.
(2008)  J.Biol.Chem.  283 : 26694

PubMed: 18614528
DOI: 10.1074/JBC.M803514200

Reaction

Chain : A
UniProt : P56524 (HDAC4_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] + acetate 3.5.1.98 PubMed:10220385, PubMed:10523670, PubMed:12032081
left-to-right PubMed:10523670, PubMed:12032081