Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1NBH

Structure of glycine N-methyltransferase complexed with S-adenosylmethionine and acetate, GNMT:SAM:Ace

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	0006111	biological_process	regulation of gluconeogenesis
A	0006544	biological_process	glycine metabolic process
A	0006546	biological_process	glycine catabolic process
A	0006730	biological_process	one-carbon metabolic process
A	0016594	molecular_function	glycine binding
A	0017174	molecular_function	glycine N-methyltransferase activity
A	0018013	biological_process	N-terminal peptidyl-glycine methylation
A	0034708	cellular_component	methyltransferase complex
A	0042802	molecular_function	identical protein binding
A	0046500	biological_process	S-adenosylmethionine metabolic process
A	0050843	biological_process	S-adenosylmethionine catabolic process
A	0051289	biological_process	protein homotetramerization
A	0098603	molecular_function	selenol Se-methyltransferase activity
A	1901052	biological_process	sarcosine metabolic process
A	1901605	biological_process	alpha-amino acid 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	0006111	biological_process	regulation of gluconeogenesis
B	0006544	biological_process	glycine metabolic process
B	0006546	biological_process	glycine catabolic process
B	0006730	biological_process	one-carbon metabolic process
B	0016594	molecular_function	glycine binding
B	0017174	molecular_function	glycine N-methyltransferase activity
B	0018013	biological_process	N-terminal peptidyl-glycine methylation
B	0034708	cellular_component	methyltransferase complex
B	0042802	molecular_function	identical protein binding
B	0046500	biological_process	S-adenosylmethionine metabolic process
B	0050843	biological_process	S-adenosylmethionine catabolic process
B	0051289	biological_process	protein homotetramerization
B	0098603	molecular_function	selenol Se-methyltransferase activity
B	1901052	biological_process	sarcosine metabolic process
B	1901605	biological_process	alpha-amino acid metabolic process
B	1904047	molecular_function	S-adenosyl-L-methionine binding
C	0005542	molecular_function	folic acid binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006111	biological_process	regulation of gluconeogenesis
C	0006544	biological_process	glycine metabolic process
C	0006546	biological_process	glycine catabolic process
C	0006730	biological_process	one-carbon metabolic process
C	0016594	molecular_function	glycine binding
C	0017174	molecular_function	glycine N-methyltransferase activity
C	0018013	biological_process	N-terminal peptidyl-glycine methylation
C	0034708	cellular_component	methyltransferase complex
C	0042802	molecular_function	identical protein binding
C	0046500	biological_process	S-adenosylmethionine metabolic process
C	0050843	biological_process	S-adenosylmethionine catabolic process
C	0051289	biological_process	protein homotetramerization
C	0098603	molecular_function	selenol Se-methyltransferase activity
C	1901052	biological_process	sarcosine metabolic process
C	1901605	biological_process	alpha-amino acid metabolic process
C	1904047	molecular_function	S-adenosyl-L-methionine binding
D	0005542	molecular_function	folic acid binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006111	biological_process	regulation of gluconeogenesis
D	0006544	biological_process	glycine metabolic process
D	0006546	biological_process	glycine catabolic process
D	0006730	biological_process	one-carbon metabolic process
D	0016594	molecular_function	glycine binding
D	0017174	molecular_function	glycine N-methyltransferase activity
D	0018013	biological_process	N-terminal peptidyl-glycine methylation
D	0034708	cellular_component	methyltransferase complex
D	0042802	molecular_function	identical protein binding
D	0046500	biological_process	S-adenosylmethionine metabolic process
D	0050843	biological_process	S-adenosylmethionine catabolic process
D	0051289	biological_process	protein homotetramerization
D	0098603	molecular_function	selenol Se-methyltransferase activity
D	1901052	biological_process	sarcosine metabolic process
D	1901605	biological_process	alpha-amino acid metabolic process
D	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	TYR33
A	ASN138
A	ARG175
A	TYR220
A	TYR242

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT B 1294

Chain	Residue
B	TYR220
B	TYR242
B	TYR33
B	ASN138
B	ARG175
B	TYR194

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT C 2294

Chain	Residue
C	TYR33
C	ASN138
C	ARG175
C	TYR220
C	TYR242

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT D 3294

Chain	Residue
D	TYR33
D	ASN138
D	ARG175
D	TYR220
D	TYR242

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE SAM A 293

Chain	Residue
A	TYR21
A	TRP30
A	ILE34
A	ARG40
A	ALA64
A	VAL69
A	ASP85
A	ALA86
A	SER87
A	MET90
A	ALA115
A	ASN116
A	TRP117
A	LEU136
A	GLY137
A	SER139
A	TYR194

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE SAM B 1293

Chain	Residue
B	TYR21
B	TRP30
B	ILE34
B	ARG40
B	ALA64
B	VAL69
B	ASP85
B	ALA86
B	SER87
B	MET90
B	ALA115
B	ASN116
B	TRP117
B	LEU136
B	GLY137
B	SER139
B	TYR194

site_id	AC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE SAM C 2293

Chain	Residue
C	TYR21
C	TRP30
C	ILE34
C	ARG40
C	ALA64
C	VAL69
C	ASP85
C	ALA86
C	SER87
C	MET90
C	ALA115
C	ASN116
C	TRP117
C	LEU136
C	GLY137
C	SER139
C	TYR194
C	HOH5037

site_id	AC8
Number of Residues	18
Details	BINDING SITE FOR RESIDUE SAM D 3293

Chain	Residue
D	TYR21
D	TRP30
D	ILE34
D	ARG40
D	ALA64
D	VAL69
D	ASP85
D	ALA86
D	SER87
D	MET90
D	ALA115
D	ASN116
D	TRP117
D	LEU136
D	GLY137
D	SER139
D	TYR194
D	HOH5247

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
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	4
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	4
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	20
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	12
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	4
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	12
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	4
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	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9QXF8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9QXF8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	16
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	1
Details	Annotated By Reference To The Literature 1xva

Chain	Residue	Details
A	GLU15

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1xva

Chain	Residue	Details
B	GLU15

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1xva

Chain	Residue	Details
C	GLU15

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1xva

Chain	Residue	Details
D	GLU15

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

site_id	MCSA3
Number of Residues	5
Details	M-CSA 23

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

site_id	MCSA4
Number of Residues	5
Details	M-CSA 23

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

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