Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3KPU

Crystal Structure of hPNMT in Complex AdoHcy and 4-quinolinol

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 Residues21
DetailsBINDING SITE FOR RESIDUE SAH A 2001
ChainResidue
ATYR27
AASP101
APHE102
ALEU103
AASN106
AASP158
AVAL159
AHIS160
AALA181
APHE182
ACYS183
ATYR35
AVAL187
AHOH2047
ATYR40
AGLY79
ASER80
AGLY81
ATHR83
ATYR85
AGLN86

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ES1 A 290
ChainResidue
ATYR35
AASN39
ATYR40
AARG44
ALYS57
APHE182
AMET258
AASP267
AVAL269
AHOH2243

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE SAH B 2002
ChainResidue
BTYR27
BTYR35
BTYR40
BGLY79
BSER80
BGLY81
BTHR83
BTYR85
BASP101
BPHE102
BLEU103
BASN106
BASP158
BVAL159
BHIS160
BALA181
BPHE182
BCYS183
BVAL187
BHOH2026
BHOH2116

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ES1 B 290
ChainResidue
BTYR35
BASN39
BTYR40
BARG44
BLYS57
BPHE182
BMET258
BASP267
BVAL269
BHOH2059
BHOH2170

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

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon