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2BZG

Crystal structure of thiopurine S-methyltransferase.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0006805biological_processxenobiotic metabolic process
A0008119molecular_functionthiopurine S-methyltransferase activity
A0008168molecular_functionmethyltransferase activity
A0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
A0016740molecular_functiontransferase activity
A0032259biological_processmethylation
A0042178biological_processxenobiotic catabolic process
A1904047molecular_functionS-adenosyl-L-methionine binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE SAH A1246
ChainResidue
ALEU26
ASER134
AILE135
AARG152
AGLY153
AHOH2036
AHOH2068
AHOH2223
AHOH2224
AHOH2225
ATRP29
ATRP33
APHE40
ALEU69
ACYS70
AGLU90
AILE91
ACYS133

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE B3P A1247
ChainResidue
AARG64
APRO111
AILE112
ATHR113
AGLU114
ATYR131
ATHR141
AASN142
AILE143
ASER229
AHOH2109
AHOH2226
AHOH2227
AHOH2228
AHOH2229
AHOH2230
AHOH2231

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING:
ChainResidueDetails
ALEU69
AGLU90
ASER134
AARG152
ATRP29

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
APHE40

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569
ChainResidueDetails
AGLY14

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS58

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PDB entries from 2024-04-17

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