3SFF

Crystal Structure of Human HDAC8 Inhibitor Complex, an Amino Acid Derived Inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000118	cellular_component	histone deacetylase complex
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0000228	cellular_component	nuclear chromosome
A	0004407	molecular_function	histone deacetylase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005694	cellular_component	chromosome
A	0005737	cellular_component	cytoplasm
A	0006325	biological_process	chromatin organization
A	0007064	biological_process	mitotic sister chromatid cohesion
A	0016787	molecular_function	hydrolase activity
A	0030544	molecular_function	Hsp70 protein binding
A	0031078	molecular_function	histone H3K14 deacetylase activity
A	0031397	biological_process	negative regulation of protein ubiquitination
A	0031647	biological_process	regulation of protein stability
A	0032129	molecular_function	histone H3K9 deacetylase activity
A	0032204	biological_process	regulation of telomere maintenance
A	0033558	molecular_function	protein lysine deacetylase activity
A	0034739	molecular_function	histone H4K16 deacetylase activity
A	0040029	biological_process	epigenetic regulation of gene expression
A	0042903	molecular_function	tubulin deacetylase activity
A	0046872	molecular_function	metal ion binding
A	0051879	molecular_function	Hsp90 protein binding
A	0140297	molecular_function	DNA-binding transcription factor binding
A	0140937	molecular_function	histone H4K12 deacetylase activity
A	0160008	molecular_function	protein decrotonylase activity
A	0160009	molecular_function	histone decrotonylase activity
A	0180032	molecular_function	histone H4K5 deacetylase activity
A	0180033	molecular_function	histone H4K48 deacetylase activity
A	1990162	molecular_function	histone H3K4 deacetylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE 0DI A 378

Chain	Residue
A	GLY140
A	ASP267
A	MET274
A	GLY303
A	GLY304
A	TYR306
A	ZN403
A	HOH665
A	HOH1009
A	TRP141
A	HIS142
A	HIS143
A	GLY151
A	PHE152
A	ASP178
A	HIS180
A	PHE208

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A 401

Chain	Residue
A	ASP176
A	ASP178
A	HIS180
A	SER199
A	LEU200

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K A 402

Chain	Residue
A	PHE189
A	THR192
A	VAL195
A	TYR225
A	HOH621
A	HOH789

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 403

Chain	Residue
A	ASP178
A	HIS180
A	ASP267
A	0DI378

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:19053282

Chain	Residue	Details
A	HIS143

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:19053282

Chain	Residue	Details
A	ASP101
A	GLY151
A	TYR306

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:17721440

Chain	Residue	Details
A	ASP178
A	HIS180
A	ASP267

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:15242608

Chain	Residue	Details
A	SER39

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