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5YJI

Co-crystal structure of Mouse Nicotinamide N-methyltransferase (NNMT) with small molecule analog of Nicotinamide

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006769biological_processnicotinamide metabolic process
A0008112molecular_functionnicotinamide N-methyltransferase activity
A0008168molecular_functionmethyltransferase activity
A0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
A0016740molecular_functiontransferase activity
A0019677biological_processNAD+ catabolic process
A0032259biological_processmethylation
A0045722biological_processpositive regulation of gluconeogenesis
A0090312biological_processpositive regulation of protein deacetylation
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
B0032259biological_processmethylation
B0045722biological_processpositive regulation of gluconeogenesis
B0090312biological_processpositive regulation of protein deacetylation
Functional Information from PDB Data
site_idAC1
Number of Residues20
Detailsbinding site for residue SAH A 301
ChainResidue
ATYR20
ATHR87
AASN90
ACYS141
AASP142
AVAL143
ATHR163
ALEU164
AALA169
A8WO302
AHOH485
ATYR25
AHOH491
AGLY63
ASER64
AGLY65
ATHR67
ATYR69
AASP85
ATYR86

site_idAC2
Number of Residues11
Detailsbinding site for residue 8WO A 302
ChainResidue
ATYR20
ATYR24
ALEU164
AALA198
ASER201
ATYR204
ASER213
ATYR242
ASER247
ASAH301
AHOH436

site_idAC3
Number of Residues19
Detailsbinding site for residue SAH B 301
ChainResidue
BTYR20
BTYR25
BGLY63
BSER64
BGLY65
BTHR67
BTYR69
BGLN70
BASP85
BTYR86
BTHR87
BASN90
BASP142
BVAL143
BTHR163
BLEU164
BCYS165
B8WO302
BHOH458

site_idAC4
Number of Residues11
Detailsbinding site for residue 8WO B 302
ChainResidue
BTYR20
BTYR24
BLEU164
BALA198
BSER201
BTYR204
BSER213
BTYR242
BSER247
BSAH301
BHOH417

Functional Information from PROSITE/UniProt
site_idPS01100
Number of Residues17
DetailsNNMT_PNMT_TEMT NNMT/PNMT/TEMT family of methyltransferases signature. LIDIGSGPTIYQLLSAC
ChainResidueDetails
ALEU59-CYS75

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29483571","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2006","submissionDatabase":"PDB data bank","title":"The Crystal Structure of Mouse Nicotinamide N-methyltransferase in complex with SAH.","authors":["Wu H.","Min J.","Zeng H.","Loppnau P.","Weigelt J.","Sundstrom M.","Arrowsmith C.H.","Edwards A.M.","Bochkarev A.","Plotnikov A.N."]}}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P40261","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsModified residue: {"description":"Citrulline; alternate","evidences":[{"source":"UniProtKB","id":"P40261","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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