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9H4Z

NNMT-SAM IN COMPLEX WITH 3b

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006769biological_processnicotinamide metabolic process
B0008112molecular_functionnicotinamide N-methyltransferase activity
B0008168molecular_functionmethyltransferase activity
B0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
B0016740molecular_functiontransferase activity
B0019677biological_processNAD+ catabolic process
B0030760molecular_functionpyridine N-methyltransferase activity
B0032259biological_processmethylation
B0045722biological_processpositive regulation of gluconeogenesis
B0090312biological_processpositive regulation of protein deacetylation
B1901847biological_processnicotinate metabolic process
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006769biological_processnicotinamide metabolic process
D0008112molecular_functionnicotinamide N-methyltransferase activity
D0008168molecular_functionmethyltransferase activity
D0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
D0016740molecular_functiontransferase activity
D0019677biological_processNAD+ catabolic process
D0030760molecular_functionpyridine N-methyltransferase activity
D0032259biological_processmethylation
D0045722biological_processpositive regulation of gluconeogenesis
D0090312biological_processpositive regulation of protein deacetylation
D1901847biological_processnicotinate metabolic process
Functional Information from PROSITE/UniProt
site_idPS01100
Number of Residues17
DetailsNNMT_PNMT_TEMT NNMT/PNMT/TEMT family of methyltransferases signature. LIDIGSGPTIYQLLSAC
ChainResidueDetails
BLEU59-CYS75

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21823666","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2006","submissionDatabase":"PDB data bank","title":"The crystal structure of human nicotinamide N-methyltransferase in complex with SAH.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21823666","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsModified residue: {"description":"Citrulline; alternate","evidences":[{"source":"PubMed","id":"30044909","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

244693

PDB entries from 2025-11-12

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