3TOB

Human MOF E350Q crystal structure with active site lysine partially acetylated

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004402	molecular_function	histone acetyltransferase activity
A	0006355	biological_process	regulation of DNA-templated transcription

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 501

Chain	Residue
A	CYS210
A	CYS213
A	HIS226
A	CYS230

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site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 502

Chain	Residue
A	ASP190

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	25
Details	ZN_FING: C2HC MYST-type => ECO:0000255|PROSITE-ProRule:PRU01063, ECO:0000269|PubMed:22020126

Chain	Residue	Details
A	LEU207-TRP232

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000303|PubMed:21217699, ECO:0000303|PubMed:22020126, ECO:0000305

Chain	Residue	Details
A	GLN350

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site_id	SWS_FT_FI3
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23

Chain	Residue	Details
A	ILE317
A	GLN324
A	SER354
A	SER363
A	LYS432

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:21691301, ECO:0000269|PubMed:22020126, ECO:0000269|PubMed:22547026, ECO:0000269|Ref.23

Chain	Residue	Details
A	ALY274

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER348

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