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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6PVS

Structure of Nicotinamide N-Methyltransferase (NNMT) in complex with inhibitor LL320

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
A0030760molecular_functionpyridine N-methyltransferase activity
A0032259biological_processmethylation
A0045722biological_processpositive regulation of gluconeogenesis
A0090312biological_processpositive regulation of protein deacetylation
A1901847biological_processnicotinate metabolic process
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
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006769biological_processnicotinamide metabolic process
C0008112molecular_functionnicotinamide N-methyltransferase activity
C0008168molecular_functionmethyltransferase activity
C0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
C0016740molecular_functiontransferase activity
C0019677biological_processNAD+ catabolic process
C0030760molecular_functionpyridine N-methyltransferase activity
C0032259biological_processmethylation
C0045722biological_processpositive regulation of gluconeogenesis
C0090312biological_processpositive regulation of protein deacetylation
C1901847biological_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 PDB Data
site_idAC1
Number of Residues24
Detailsbinding site for residue P0V A 301
ChainResidue
ATYR20
ASER87
AASN90
AASP142
AVAL143
ATHR163
ALEU164
ACYS165
AASP167
ASER201
ATYR203
ATYR25
ATYR204
ASER213
ATYR242
AHOH421
AHOH423
AGLY63
ASER64
AGLY65
ATHR67
ATYR69
AASP85
ATYR86
site_idAC2
Number of Residues26
Detailsbinding site for residue P0V B 301
ChainResidue
BTYR11
BTYR20
BTYR25
BGLY63
BSER64
BGLY65
BTHR67
BTYR69
BASP85
BTYR86
BSER87
BASN90
BASP142
BVAL143
BTHR163
BLEU164
BCYS165
BASP167
BASP197
BALA198
BSER201
BTYR204
BSER213
BTYR242
BHOH417
BHOH425
site_idAC3
Number of Residues24
Detailsbinding site for residue P0V C 301
ChainResidue
CTYR20
CTYR25
CGLY63
CSER64
CGLY65
CTHR67
CTYR69
CASP85
CTYR86
CSER87
CASN90
CCYS141
CASP142
CVAL143
CTHR163
CLEU164
CASP167
CALA169
CALA198
CSER201
CTYR203
CTYR204
CSER213
CTYR242
site_idAC4
Number of Residues19
Detailsbinding site for residue P0V D 301
ChainResidue
DTYR20
DTYR25
DGLY63
DSER64
DTHR67
DTYR69
DASP85
DTYR86
DSER87
DASN90
DASP142
DVAL143
DTHR163
DLEU164
DALA198
DSER201
DTYR204
DSER213
DTYR242
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_FI2
Number of Residues8
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_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21823666","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues12
DetailsModified residue: {"description":"Citrulline; alternate","evidences":[{"source":"PubMed","id":"30044909","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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PDB entries from 2025-11-05

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