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6I6K

Papaver somniferum O-methyltransferase 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0008168molecular_functionmethyltransferase activity
A0008171molecular_functionO-methyltransferase activity
A0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
A0009708biological_processbenzyl isoquinoline alkaloid biosynthetic process
A0009820biological_processalkaloid metabolic process
A0016740molecular_functiontransferase activity
A0019438biological_processobsolete aromatic compound biosynthetic process
A0030762molecular_functiontetrahydrocolumbamine 2-O-methyltransferase activity
A0030777molecular_function(S)-scoulerine 9-O-methyltransferase activity
A0032259biological_processmethylation
A0046983molecular_functionprotein dimerization activity
B0008168molecular_functionmethyltransferase activity
B0008171molecular_functionO-methyltransferase activity
B0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
B0009708biological_processbenzyl isoquinoline alkaloid biosynthetic process
B0009820biological_processalkaloid metabolic process
B0016740molecular_functiontransferase activity
B0019438biological_processobsolete aromatic compound biosynthetic process
B0030762molecular_functiontetrahydrocolumbamine 2-O-methyltransferase activity
B0030777molecular_function(S)-scoulerine 9-O-methyltransferase activity
B0032259biological_processmethylation
B0046983molecular_functionprotein dimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue SLX A 401
ChainResidue
AGLU153
AILE342
ALEU347
ASAH402
AHOH519
AHOH541
ATHR157
APHE203
AMET207
APHE210
ATRP293
AHIS296
AASP297
AASN339

site_idAC2
Number of Residues23
Detailsbinding site for residue SAH A 402
ChainResidue
APHE190
APHE203
AMET207
ASER211
AGLY235
AGLY237
AASP258
ALEU259
AVAL262
AASP278
AMET279
APHE280
ALYS292
ATRP293
AASP297
ASLX401
AHOH518
AHOH527
AHOH542
AHOH579
AHOH621
AHOH653
AHOH671

site_idAC3
Number of Residues15
Detailsbinding site for residue SLX B 401
ChainResidue
BGLU153
BPHE156
BPHE203
BPHE210
BTRP293
BHIS296
BASP297
BPHE325
BASN339
BILE342
BPRO343
BLEU347
BSAH402
BHOH524
BHOH543

site_idAC4
Number of Residues22
Detailsbinding site for residue SAH B 402
ChainResidue
BPHE190
BMET207
BSER211
BGLY235
BGLY237
BASP258
BLEU259
BVAL262
BASP278
BMET279
BPHE280
BLYS292
BTRP293
BASP297
BSLX401
BHOH514
BHOH517
BHOH538
BHOH604
BHOH631
BHOH642
BHOH645

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01020, ECO:0000269|DOI:10.1021/acscatal.9b01038
ChainResidueDetails
AHIS296
BHIS296

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:6I6K, ECO:0007744|PDB:6I6N
ChainResidueDetails
AGLU153
BGLU153

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q5C9L7
ChainResidueDetails
AMET207
BMET207

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|DOI:10.1021/acscatal.9b01038, ECO:0007744|PDB:6I6K, ECO:0007744|PDB:6I6N
ChainResidueDetails
ASER211
BHIS296
AGLY235
AASP278
ALYS292
AHIS296
BSER211
BGLY235
BASP278
BLYS292

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01020, ECO:0000269|DOI:10.1021/acscatal.9b01038, ECO:0007744|PDB:6I6K, ECO:0007744|PDB:6I6N
ChainResidueDetails
AASP258
BASP258

218853

PDB entries from 2024-04-24

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