7WMC

Crystal structure of macrocyclic peptide 1 bound to human Nicotinamide N-methyltransferase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006769	biological_process	nicotinamide metabolic process
A	0008112	molecular_function	nicotinamide N-methyltransferase activity
A	0008168	molecular_function	methyltransferase activity
A	0008757	molecular_function	S-adenosylmethionine-dependent methyltransferase activity
A	0009410	biological_process	response to xenobiotic stimulus
A	0010243	biological_process	response to organonitrogen compound
A	0030760	molecular_function	pyridine N-methyltransferase activity
A	0031100	biological_process	animal organ regeneration
A	0032259	biological_process	methylation
A	0034356	biological_process	NAD biosynthesis via nicotinamide riboside salvage pathway
A	0045722	biological_process	positive regulation of gluconeogenesis
A	0090312	biological_process	positive regulation of protein deacetylation
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006769	biological_process	nicotinamide metabolic process
B	0008112	molecular_function	nicotinamide N-methyltransferase activity
B	0008168	molecular_function	methyltransferase activity
B	0008757	molecular_function	S-adenosylmethionine-dependent methyltransferase activity
B	0009410	biological_process	response to xenobiotic stimulus
B	0010243	biological_process	response to organonitrogen compound
B	0030760	molecular_function	pyridine N-methyltransferase activity
B	0031100	biological_process	animal organ regeneration
B	0032259	biological_process	methylation
B	0034356	biological_process	NAD biosynthesis via nicotinamide riboside salvage pathway
B	0045722	biological_process	positive regulation of gluconeogenesis
B	0090312	biological_process	positive regulation of protein deacetylation

Functional Information from PROSITE/UniProt

site_id	PS01100
Number of Residues	17
Details	NNMT_PNMT_TEMT NNMT/PNMT/TEMT family of methyltransferases signature. LIDIGSGPTIYQLLSAC

Chain	Residue	Details
A	LEU59-CYS75

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269|PubMed:21823666, ECO:0000269|Ref.12

Chain	Residue	Details
A	TYR20
B	TYR25
B	GLY63
B	TYR69
B	ASP85
B	ASN90
B	ASP142
B	THR163
A	TYR25
A	GLY63
A	TYR69
A	ASP85
A	ASN90
A	ASP142
A	THR163
B	TYR20

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:21823666

Chain	Residue	Details
A	ASP197
A	SER213
B	ASP197
B	SER213

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: Citrulline; alternate => ECO:0000269|PubMed:30044909

Chain	Residue	Details
A	ARG18
A	ARG132
A	ARG181
B	ARG18
B	ARG132
B	ARG181

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS39
B	LYS39

---