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3HCC

Crystal Structure of hPNMT in Complex With anti-9-amino-5-(trifluromethyl) benzonorbornene and AdoHcy

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 Residues15
DetailsBINDING SITE FOR RESIDUE LT3 A 2001
ChainResidue
ATYR35
AMET258
AASP267
AVAL269
AVAL272
AHOH291
AHOH369
AASN39
ATYR40
AARG44
AVAL53
ALYS57
APHE182
AGLU219
ATYR222

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE SAH A 3001
ChainResidue
ATYR27
ATYR35
ATYR40
AGLY79
ASER80
AGLY81
ATHR83
ATYR85
AASP101
APHE102
ALEU103
AASN106
AASP158
AVAL159
AHIS160
AALA181
APHE182
ACYS183
AVAL187
AHOH358

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE LT3 B 2002
ChainResidue
BTYR35
BTYR40
BARG44
BVAL53
BPHE182
BGLU219
BTYR222
BMET258
BASP267
BVAL269
BVAL272
BHOH320
BHOH331

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE SAH B 3002
ChainResidue
BTYR27
BTYR35
BTYR40
BGLY79
BSER80
BGLY81
BTHR83
BTYR85
BASP101
BPHE102
BLEU103
BASN106
BILE157
BASP158
BVAL159
BHIS160
BALA181
BPHE182
BCYS183
BVAL187
BHOH320
BHOH333

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

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PDB entries from 2024-07-10

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