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5KPG

Pavine N-methyltransferase in complex with S-adenosylhomocysteine pH 7

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0008168molecular_functionmethyltransferase activity
A0032259biological_processmethylation
B0005737cellular_componentcytoplasm
B0008168molecular_functionmethyltransferase activity
B0032259biological_processmethylation
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue SAH A 401
ChainResidue
APHE96
AVAL201
AALA202
ALEU203
AHIS206
AHOH541
AHOH651
AHOH663
AHOH681
AHOH683
AHOH688
ASER97
AHOH691
AHOH711
AHOH728
AHOH751
AGLY135
ASER140
AASN159
AGLN163
AGLU184
AASP185
AVAL186

site_idAC2
Number of Residues18
Detailsbinding site for residue SAH B 401
ChainResidue
BPHE96
BSER97
BGLY135
BSER140
BASN159
BGLN163
BGLU184
BASP185
BVAL186
BVAL201
BALA202
BLEU203
BHOH510
BHOH556
BHOH578
BHOH592
BHOH631
BHOH649

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P9WPB7
ChainResidueDetails
ACYS331
BCYS331

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:27573242, ECO:0007744|PDB:5KOC
ChainResidueDetails
AGLN163
AASP185
AVAL186
AVAL201
BPHE96
BSER97
BGLY135
BASN159
BGLN163
BASP185
BVAL186
BVAL201
AGLY135
AASN159
APHE96
ASER97

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:27573242, ECO:0007744|PDB:5KOK
ChainResidueDetails
AGLU205
BGLU205

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PDB entries from 2024-06-12

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