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1HNN

CRYSTAL STRUCTURE OF HUMAN PNMT COMPLEXED WITH SK&F 29661 AND ADOHCY(SAH)

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 2001
ChainResidue
ATYR27
APHE102
ALEU103
AASN106
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 2002
ChainResidue
BTYR527
BTYR535
BTYR540
BGLY579
BSER580
BGLY581
BTHR583
BTYR585
BASP601
BPHE602
BLEU603
BASN606
BASP658
BVAL659
BALA681
BPHE682
BCYS683
BVAL687
BHOH1035

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SKF A 3001
ChainResidue
ATYR35
AASN39
ATYR40
AARG44
AVAL53
ALYS57
APHE182
AGLU219
AMET258
AASP267
AHOH1022

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SKF B 3002
ChainResidue
BTYR535
BASN539
BTYR540
BARG544
BVAL553
BLYS557
BPHE682
BGLU719
BMET758
BASP767
BVAL769
BHOH1023

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
BASP601
BASN606
BALA681
ATYR40
ATYR85
AASP101
AASN106
AALA181
BTYR535
BTYR540
BTYR585

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17845018, ECO:0007744|PDB:2G70, ECO:0007744|PDB:2G72
ChainResidueDetails
AGLY79
AASP158
BGLY579
BASP658

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16363801, ECO:0007744|PDB:2AN4
ChainResidueDetails
AGLU219
AASP267
BGLU719
BASP767

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER7
BSER507

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 1005
ChainResidueDetails
AGLU185proton acceptor
AGLU219proton acceptor

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PDB entries from 2024-07-10

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