Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4QPP

The Crystal Structure of Human HMT1 hnRNP methyltransferase-like protein 6 in complex with compound DS-421 (2-{4-[3-CHLORO-2-(2-METHOXYPHENYL)-1H-INDOL-5-YL]PIPERIDIN-1-YL}-N-METHYLETHANAMINE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0003682	molecular_function	chromatin binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005730	cellular_component	nucleolus
A	0006281	biological_process	DNA repair
A	0006284	biological_process	base-excision repair
A	0006325	biological_process	chromatin organization
A	0006338	biological_process	chromatin remodeling
A	0008168	molecular_function	methyltransferase activity
A	0008170	molecular_function	N-methyltransferase activity
A	0008469	molecular_function	histone arginine N-methyltransferase activity
A	0010821	biological_process	regulation of mitochondrion organization
A	0016274	molecular_function	protein-arginine N-methyltransferase activity
A	0018216	biological_process	peptidyl-arginine methylation
A	0032259	biological_process	methylation
A	0035241	molecular_function	protein-arginine omega-N monomethyltransferase activity
A	0035242	molecular_function	protein-arginine omega-N asymmetric methyltransferase activity
A	0036211	biological_process	protein modification process
A	0042054	molecular_function	histone methyltransferase activity
A	0042393	molecular_function	histone binding
A	0044020	molecular_function	histone H4R3 methyltransferase activity
A	0045652	biological_process	regulation of megakaryocyte differentiation
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0070611	molecular_function	histone H3R2 methyltransferase activity
A	0070612	molecular_function	histone H2AR3 methyltransferase activity
A	0090398	biological_process	cellular senescence
A	0140938	molecular_function	histone H3 methyltransferase activity
A	1901796	biological_process	regulation of signal transduction by p53 class mediator
A	2000059	biological_process	negative regulation of ubiquitin-dependent protein catabolic process
B	0000122	biological_process	negative regulation of transcription by RNA polymerase II
B	0003682	molecular_function	chromatin binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005730	cellular_component	nucleolus
B	0006281	biological_process	DNA repair
B	0006284	biological_process	base-excision repair
B	0006325	biological_process	chromatin organization
B	0006338	biological_process	chromatin remodeling
B	0008168	molecular_function	methyltransferase activity
B	0008170	molecular_function	N-methyltransferase activity
B	0008469	molecular_function	histone arginine N-methyltransferase activity
B	0010821	biological_process	regulation of mitochondrion organization
B	0016274	molecular_function	protein-arginine N-methyltransferase activity
B	0018216	biological_process	peptidyl-arginine methylation
B	0032259	biological_process	methylation
B	0035241	molecular_function	protein-arginine omega-N monomethyltransferase activity
B	0035242	molecular_function	protein-arginine omega-N asymmetric methyltransferase activity
B	0036211	biological_process	protein modification process
B	0042054	molecular_function	histone methyltransferase activity
B	0042393	molecular_function	histone binding
B	0044020	molecular_function	histone H4R3 methyltransferase activity
B	0045652	biological_process	regulation of megakaryocyte differentiation
B	0045892	biological_process	negative regulation of DNA-templated transcription
B	0070611	molecular_function	histone H3R2 methyltransferase activity
B	0070612	molecular_function	histone H2AR3 methyltransferase activity
B	0090398	biological_process	cellular senescence
B	0140938	molecular_function	histone H3 methyltransferase activity
B	1901796	biological_process	regulation of signal transduction by p53 class mediator
B	2000059	biological_process	negative regulation of ubiquitin-dependent protein catabolic process
C	0000122	biological_process	negative regulation of transcription by RNA polymerase II
C	0003682	molecular_function	chromatin binding
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005730	cellular_component	nucleolus
C	0006281	biological_process	DNA repair
C	0006284	biological_process	base-excision repair
C	0006325	biological_process	chromatin organization
C	0006338	biological_process	chromatin remodeling
C	0008168	molecular_function	methyltransferase activity
C	0008170	molecular_function	N-methyltransferase activity
C	0008469	molecular_function	histone arginine N-methyltransferase activity
C	0010821	biological_process	regulation of mitochondrion organization
C	0016274	molecular_function	protein-arginine N-methyltransferase activity
C	0018216	biological_process	peptidyl-arginine methylation
C	0032259	biological_process	methylation
C	0035241	molecular_function	protein-arginine omega-N monomethyltransferase activity
C	0035242	molecular_function	protein-arginine omega-N asymmetric methyltransferase activity
C	0036211	biological_process	protein modification process
C	0042054	molecular_function	histone methyltransferase activity
C	0042393	molecular_function	histone binding
C	0044020	molecular_function	histone H4R3 methyltransferase activity
C	0045652	biological_process	regulation of megakaryocyte differentiation
C	0045892	biological_process	negative regulation of DNA-templated transcription
C	0070611	molecular_function	histone H3R2 methyltransferase activity
C	0070612	molecular_function	histone H2AR3 methyltransferase activity
C	0090398	biological_process	cellular senescence
C	0140938	molecular_function	histone H3 methyltransferase activity
C	1901796	biological_process	regulation of signal transduction by p53 class mediator
C	2000059	biological_process	negative regulation of ubiquitin-dependent protein catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE SAH A 1000

Chain	Residue
A	HIS57
A	SER114
A	PRO139
A	VAL140
A	GLU141
A	GLU155
A	MET166
A	SER169
A	HOH1108
A	HOH1114
A	HOH1115
A	MET60
A	ARG66
A	GLY90
A	ALA91
A	ILE95
A	LEU96
A	GLU112
A	ALA113

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 36S A 1001

Chain	Residue
A	LEU162
A	GLU264
A	LEU267
A	PRO345
A	PRO350
A	ARG351
A	ARG352

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE SAH B 1000

Chain	Residue
B	HIS57
B	MET60
B	ARG66
B	GLY90
B	ALA91
B	LEU96
B	GLU112
B	ALA113
B	SER114
B	PRO139
B	VAL140
B	GLU141
B	GLU155
B	MET166
B	SER169
B	HOH1113
B	HOH1117
B	HOH1118
B	HOH1169

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 36S B 1001

Chain	Residue
B	LEU162
B	SER168
B	GLU264
B	LEU267
B	LEU344
B	PRO345
B	PRO350
B	ARG352

site_id	AC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE SAH C 1000

Chain	Residue
C	HIS57
C	MET60
C	ARG66
C	GLY90
C	ALA91
C	LEU96
C	GLU112
C	ALA113
C	SER114
C	PRO139
C	VAL140
C	GLU141
C	GLU155
C	MET166
C	SER169
C	HOH1120
C	HOH1122
C	HOH1123
C	HOH1178

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 36S C 1001

Chain	Residue
C	LEU162
C	GLU264
C	LEU267
C	PRO345
C	PRO350
C	ARG351
C	ARG352
C	LEU353

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: ACT_SITE => ECO:0000250

Chain	Residue	Details
A	GLU155
A	GLU164
B	GLU155
B	GLU164
C	GLU155
C	GLU164

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	HIS57
B	HIS57
C	HIS57

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING:

Chain	Residue	Details
A	ARG66
C	GLY90
C	GLU112
C	GLU141
A	GLY90
A	GLU112
A	GLU141
B	ARG66
B	GLY90
B	GLU112
B	GLU141
C	ARG66

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:18691976, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	THR21
B	THR21
C	THR21

site_id	SWS_FT_FI5
Number of Residues	9
Details	MOD_RES: Asymmetric dimethylarginine; by autocatalysis => ECO:0000269\|PubMed:23866860

Chain	Residue	Details
A	ARG29
A	ARG35
A	ARG37
B	ARG29
B	ARG35
B	ARG37
C	ARG29
C	ARG35
C	ARG37

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