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3BGI

Thiopurine S-Methyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0008119molecular_functionthiopurine S-methyltransferase activity
A0008168molecular_functionmethyltransferase activity
A0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
A0032259biological_processmethylation
B0005737cellular_componentcytoplasm
B0008119molecular_functionthiopurine S-methyltransferase activity
B0008168molecular_functionmethyltransferase activity
B0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
B0032259biological_processmethylation
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE SAH A 300
ChainResidue
ALEU21
ASER129
AILE130
AARG147
AALA152
AHOH326
AHOH475
AHOH504
ATRP24
ATRP28
AHIS41
ALEU64
ACYS65
AGLU85
AILE86
ACYS128

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE SAH B 300
ChainResidue
BLEU21
BTRP24
BTRP28
BLEU64
BCYS65
BGLU85
BILE86
BCYS128
BSER129
BILE130
BPHE131
BARG147
BALA152
BHOH356
BHOH361
BHOH470
BHOH472
BHOH506

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING:
ChainResidueDetails
ATRP24
BGLU85
BSER129
BARG147
APHE35
ALEU64
AGLU85
ASER129
AARG147
BTRP24
BPHE35
BLEU64

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER34
BSER34

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P51580
ChainResidueDetails
ALYS53
BLYS53

220113

PDB entries from 2024-05-22

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