Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7CMR

The Crystal Structure of human MYST1 from Biortus.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000123	cellular_component	histone acetyltransferase complex
A	0000776	cellular_component	kinetochore
A	0000785	cellular_component	chromatin
A	0003682	molecular_function	chromatin binding
A	0003712	molecular_function	transcription coregulator activity
A	0003713	molecular_function	transcription coactivator activity
A	0004402	molecular_function	histone acetyltransferase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005694	cellular_component	chromosome
A	0005739	cellular_component	mitochondrion
A	0006325	biological_process	chromatin organization
A	0006355	biological_process	regulation of DNA-templated transcription
A	0006357	biological_process	regulation of transcription by RNA polymerase II
A	0009048	biological_process	dosage compensation by inactivation of X chromosome
A	0010485	molecular_function	histone H4 acetyltransferase activity
A	0010506	biological_process	regulation of autophagy
A	0010557	biological_process	positive regulation of macromolecule biosynthetic process
A	0010719	biological_process	negative regulation of epithelial to mesenchymal transition
A	0016363	cellular_component	nuclear matrix
A	0016407	molecular_function	acetyltransferase activity
A	0016746	molecular_function	acyltransferase activity
A	0019899	molecular_function	enzyme binding
A	0022008	biological_process	neurogenesis
A	0030099	biological_process	myeloid cell differentiation
A	0032480	biological_process	negative regulation of type I interferon production
A	0032931	molecular_function	histone H3K56 acetyltransferase activity
A	0035166	biological_process	post-embryonic hemopoiesis
A	0035267	cellular_component	NuA4 histone acetyltransferase complex
A	0036408	molecular_function	histone H3K14 acetyltransferase activity
A	0043992	molecular_function	histone H3K9 acetyltransferase activity
A	0043993	molecular_function	histone H3K18 acetyltransferase activity
A	0043994	molecular_function	histone H3K23 acetyltransferase activity
A	0043995	molecular_function	histone H4K5 acetyltransferase activity
A	0043996	molecular_function	histone H4K8 acetyltransferase activity
A	0043997	molecular_function	histone H4K12 acetyltransferase activity
A	0043999	molecular_function	histone H2AK5 acetyltransferase activity
A	0044012	molecular_function	histone H2AK9 acetyltransferase activity
A	0044014	molecular_function	histone H2BK5 acetyltransferase activity
A	0044015	molecular_function	histone H2BK12 acetyltransferase activity
A	0044016	molecular_function	histone H3K4 acetyltransferase activity
A	0044017	molecular_function	histone H3K27 acetyltransferase activity
A	0044018	molecular_function	histone H3K36 acetyltransferase activity
A	0044545	cellular_component	NSL complex
A	0045815	biological_process	transcription initiation-coupled chromatin remodeling
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0045893	biological_process	positive regulation of DNA-templated transcription
A	0045935	biological_process	positive regulation of nucleobase-containing compound metabolic process
A	0046872	molecular_function	metal ion binding
A	0046972	molecular_function	histone H4K16 acetyltransferase activity
A	0048477	biological_process	oogenesis
A	0050684	biological_process	regulation of mRNA processing
A	0060261	biological_process	positive regulation of transcription initiation by RNA polymerase II
A	0061629	molecular_function	RNA polymerase II-specific DNA-binding transcription factor binding
A	0061733	molecular_function	peptide-lysine-N-acetyltransferase activity
A	0061920	molecular_function	protein propionyltransferase activity
A	0071339	cellular_component	MLL1 complex
A	0072487	cellular_component	MSL complex
A	0140908	molecular_function	histone H3K122 acetyltransferase activity
A	0141002	molecular_function	histone H4K16 propionyltransferase activity
A	1902726	biological_process	positive regulation of skeletal muscle satellite cell differentiation
A	1903108	biological_process	regulation of mitochondrial transcription
A	1990841	molecular_function	promoter-specific chromatin binding

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

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305\|PubMed:21217699, ECO:0000305\|PubMed:27768893, ECO:0000305\|PubMed:33657400

Chain	Residue	Details
A	GLU350

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:21217699, ECO:0000269\|PubMed:21691301, ECO:0000269\|PubMed:22020126, ECO:0000269\|PubMed:27382063, ECO:0000269\|PubMed:29321206, ECO:0000269\|Ref.33, ECO:0007744\|PDB:2GIV, ECO:0007744\|PDB:2PQ8, ECO:0007744\|PDB:2Y0M, ECO:0007744\|PDB:3QAH, ECO:0007744\|PDB:3TOA, ECO:0007744\|PDB:3TOB, ECO:0007744\|PDB:4DNC, ECO:0007744\|PDB:5J8C, ECO:0007744\|PDB:5J8F, ECO:0007744\|PDB:5WCI

Chain	Residue	Details
A	CYS210
A	CYS213
A	HIS226
A	CYS230

site_id	SWS_FT_FI4
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269\|PubMed:29321206, ECO:0007744\|PDB:5WCI

Chain	Residue	Details
A	ILE317
A	THR319
A	ARG325
A	GLY329
A	LYS330
A	SER354
A	SER363

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:21217699, ECO:0000269\|Ref.33, ECO:0007744\|PDB:2GIV, ECO:0007744\|PDB:2Y0M

Chain	Residue	Details
A	ARG326
A	GLY327

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:21217699, ECO:0007744\|PDB:2Y0M

Chain	Residue	Details
A	TYR408
A	LYS432

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0007744\|PubMed:19413330, ECO:0007744\|PubMed:22814378

Chain	Residue	Details
A	ALA2

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:Q5XI06

Chain	Residue	Details
A	SER37
A	SER42

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS113

site_id	SWS_FT_FI10
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\|PubMed:22918831, ECO:0000269\|PubMed:27382063, ECO:0000269\|Ref.33, ECO:0007744\|PDB:2GIV

Chain	Residue	Details
A	ALY274

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER348

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)