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2G70

Structure of human PNMT in complex with inhibitor 3-hydroxymethyl-7-nitro-THIQ and AdoMet (SAM)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004603molecular_functionphenylethanolamine N-methyltransferase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0008168molecular_functionmethyltransferase activity
A0016740molecular_functiontransferase activity
A0032259biological_processmethylation
A0042418biological_processepinephrine biosynthetic process
A0042423biological_processcatecholamine biosynthetic process
B0004603molecular_functionphenylethanolamine N-methyltransferase activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0008168molecular_functionmethyltransferase activity
B0016740molecular_functiontransferase activity
B0032259biological_processmethylation
B0042418biological_processepinephrine biosynthetic process
B0042423biological_processcatecholamine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 502
ChainResidue
BGLU69
BARG206
BGLY208
BHIS210
BGLN278

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE SAM A 2001
ChainResidue
AGLY81
ATHR83
ATYR85
AASP101
APHE102
ALEU103
AASN106
AASP158
AVAL159
AALA181
APHE182
ACYS183
AVAL187
ATYR222
AHNT5001
ATYR35
ATYR40
AGLY79
ASER80

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE SAM B 2002
ChainResidue
BTYR35
BTYR40
BGLY79
BSER80
BGLY81
BTHR83
BTYR85
BASP101
BPHE102
BLEU103
BASN106
BILE157
BASP158
BVAL159
BALA181
BPHE182
BCYS183
BVAL187
BTYR222
BHNT5002

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HNT A 5001
ChainResidue
ATYR35
AASN39
ATYR40
AARG44
AVAL53
ALYS57
APHE182
AALA186
AGLU219
ATYR222
AMET258
AASP267
ASAM2001
AHOH5009
AHOH5017

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HNT B 5002
ChainResidue
BTYR35
BASN39
BTYR40
BARG44
BVAL53
BLYS57
BPHE182
BALA186
BGLU219
BMET258
BASP267
BVAL269
BSAM2002

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE HNT A 5003
ChainResidue
AARG240
AVAL250
AARG251
ALEU253
AHOH5032
BARG240
BVAL250
BASP252
BLEU253

Functional Information from PROSITE/UniProt
site_idPS01100
Number of Residues17
DetailsNNMT_PNMT_TEMT NNMT/PNMT/TEMT family of methyltransferases signature. LIDIGSGPTVYQLLSAC
ChainResidueDetails
ALEU75-CYS91

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16363801","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17845018","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2AN4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G70","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17845018","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2G70","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16363801","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2AN4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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