Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1XVA

METHYLTRANSFERASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005542	molecular_function	folic acid binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005977	biological_process	glycogen metabolic process
A	0006111	biological_process	regulation of gluconeogenesis
A	0006520	biological_process	amino acid metabolic process
A	0006544	biological_process	glycine metabolic process
A	0006555	biological_process	methionine metabolic process
A	0006730	biological_process	one-carbon metabolic process
A	0008168	molecular_function	methyltransferase activity
A	0008757	molecular_function	S-adenosylmethionine-dependent methyltransferase activity
A	0016594	molecular_function	glycine binding
A	0016740	molecular_function	transferase activity
A	0017174	molecular_function	glycine N-methyltransferase activity
A	0032259	biological_process	methylation
A	0034708	cellular_component	methyltransferase complex
A	0042802	molecular_function	identical protein binding
A	0046498	biological_process	S-adenosylhomocysteine metabolic process
A	0046500	biological_process	S-adenosylmethionine metabolic process
A	0051289	biological_process	protein homotetramerization
A	0098603	molecular_function	selenol Se-methyltransferase activity
A	1901052	biological_process	sarcosine metabolic process
A	1904047	molecular_function	S-adenosyl-L-methionine binding
B	0005542	molecular_function	folic acid binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005977	biological_process	glycogen metabolic process
B	0006111	biological_process	regulation of gluconeogenesis
B	0006520	biological_process	amino acid metabolic process
B	0006544	biological_process	glycine metabolic process
B	0006555	biological_process	methionine metabolic process
B	0006730	biological_process	one-carbon metabolic process
B	0008168	molecular_function	methyltransferase activity
B	0008757	molecular_function	S-adenosylmethionine-dependent methyltransferase activity
B	0016594	molecular_function	glycine binding
B	0016740	molecular_function	transferase activity
B	0017174	molecular_function	glycine N-methyltransferase activity
B	0032259	biological_process	methylation
B	0034708	cellular_component	methyltransferase complex
B	0042802	molecular_function	identical protein binding
B	0046498	biological_process	S-adenosylhomocysteine metabolic process
B	0046500	biological_process	S-adenosylmethionine metabolic process
B	0051289	biological_process	protein homotetramerization
B	0098603	molecular_function	selenol Se-methyltransferase activity
B	1901052	biological_process	sarcosine metabolic process
B	1904047	molecular_function	S-adenosyl-L-methionine binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT A 294

Chain	Residue
A	TRP30
A	LEU240
A	SAM293
B	ALA13
B	ALA14

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT B 294

Chain	Residue
B	ILE34
B	LEU240
B	SAM293
A	ALA13
A	ALA14
A	GLU15
B	TRP30

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE SAM A 293

Chain	Residue
A	TYR33
A	ALA64
A	VAL69
A	ASP70
A	LEU136
A	GLY137
A	SER139
A	HIS142
A	ARG175
A	PRO187
A	GLY189
A	ILE202
A	TYR242
A	ACT294
A	HOH343
A	HOH353
B	GLU15

site_id	AC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE SAM B 293

Chain	Residue
A	GLU15
B	TYR33
B	ALA64
B	ASP70
B	LEU136
B	GLY137
B	ASN138
B	SER139
B	HIS142
B	ARG175
B	PRO187
B	TYR194
B	ILE202
B	TYR220
B	TYR242
B	TYR283
B	ACT294
B	HOH311
B	HOH314

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22037183","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3THR","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3THS","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22037183","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3THS","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12859184","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NBH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12859184","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NBI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8810903","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XVA","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12859184","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8810903","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XVA","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NBI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12859184","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8810903","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NBI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XVA","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"N-acetylvaline","evidences":[{"source":"PubMed","id":"2822402","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9QXF8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9QXF8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9QXF8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	a catalytic site defined by CSA, PubMed 8810903

Chain	Residue	Details
A	TYR21
A	GLY137
A	TYR194
A	ARG175
A	HIS142

site_id	CSA2
Number of Residues	5
Details	a catalytic site defined by CSA, PubMed 8810903

Chain	Residue	Details
B	GLY137
B	ARG175
B	TYR194
B	TYR21
B	HIS142

site_id	MCSA1
Number of Residues	5
Details	M-CSA 23

Chain	Residue	Details
A	TYR21	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
A	GLY137	electrostatic stabiliser, hydrogen bond acceptor
A	HIS142	activator
A	ARG175	electrostatic stabiliser
A	TYR194	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor

site_id	MCSA2
Number of Residues	5
Details	M-CSA 23

Chain	Residue	Details
B	TYR21	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
B	GLY137	electrostatic stabiliser, hydrogen bond acceptor
B	HIS142	activator
B	ARG175	electrostatic stabiliser
B	TYR194	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)