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3KPJ

Crystal Structure of hPNMT in Complex AdoHcy and Bound Phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004603molecular_functionphenylethanolamine N-methyltransferase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0008168molecular_functionmethyltransferase activity
A0032259biological_processmethylation
A0042418biological_processepinephrine biosynthetic process
A0042423biological_processcatecholamine biosynthetic process
B0004603molecular_functionphenylethanolamine N-methyltransferase activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0008168molecular_functionmethyltransferase activity
B0032259biological_processmethylation
B0042418biological_processepinephrine biosynthetic process
B0042423biological_processcatecholamine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE SAH A 3001
ChainResidue
ATYR27
APHE102
AASN106
AILE157
AASP158
AVAL159
AHIS160
AALA181
APHE182
ACYS183
AVAL187
ATYR35
ATYR40
AGLY79
ASER80
AGLY81
ATHR83
ATYR85
AASP101

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE SAH B 3002
ChainResidue
BTYR35
BTYR40
BGLY79
BSER80
BGLY81
BTHR83
BTYR85
BASP101
BPHE102
BLEU103
BASN106
BILE157
BASP158
BVAL159
BHIS160
BALA181
BPHE182
BCYS183
BVAL187

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 290
ChainResidue
AASN39
ALYS57
APHE182
AHOH291

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 290
ChainResidue
BASN39
BARG44
BLYS57
BPHE182

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: BINDING => ECO:0000269|PubMed:16363801, ECO:0000269|PubMed:17845018, ECO:0007744|PDB:2AN4, ECO:0007744|PDB:2G70, ECO:0007744|PDB:2G72
ChainResidueDetails
ATYR35
BASP101
BASN106
BALA181
ATYR40
ATYR85
AASP101
AASN106
AALA181
BTYR35
BTYR40
BTYR85

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17845018, ECO:0007744|PDB:2G70, ECO:0007744|PDB:2G72
ChainResidueDetails
AGLY79
AASP158
BGLY79
BASP158

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16363801, ECO:0007744|PDB:2AN4
ChainResidueDetails
AGLU219
AASP267
BGLU219
BASP267

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER7
BSER7

220113

PDB entries from 2024-05-22

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