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6GKV

Crystal structure of Coclaurine N-Methyltransferase (CNMT) bound to N-methylheliamine and SAH

Functional Information from GO Data
ChainGOidnamespacecontents
A0008168molecular_functionmethyltransferase activity
A0030776molecular_function(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase activity
A0032259biological_processmethylation
B0008168molecular_functionmethyltransferase activity
B0030776molecular_function(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase activity
B0032259biological_processmethylation
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue SAH A 501
ChainResidue
AVAL73
AASP187
AILE188
AILE203
AGLU204
ALEU205
AMET209
AHOH603
ATYR81
AGLY98
ASER99
AGLY137
ACYS138
AGLY139
AASN161
AGLN165

site_idAC2
Number of Residues8
Detailsbinding site for residue F2W A 502
ChainResidue
AGLU204
APHE257
AILE264
AASN294
APHE332
AGLY336
AMET339
APHE340

site_idAC3
Number of Residues8
Detailsbinding site for residue F2W B 401
ChainResidue
BGLU204
BPHE257
BMET262
BPHE290
BASN294
BPHE332
BGLY336
BPHE340

site_idAC4
Number of Residues17
Detailsbinding site for residue SAH B 402
ChainResidue
BASP77
BTYR81
BGLY98
BSER99
BGLY137
BCYS138
BGLY139
BTHR160
BASN161
BGLN165
BALA186
BASP187
BILE188
BTHR189
BILE203
BGLU204
BHOH508

226707

PDB entries from 2024-10-30

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