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2EFJ

The structure of 1,7 dimethylxanthine methyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0008168molecular_functionmethyltransferase activity
A0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
A0009820biological_processalkaloid metabolic process
A0032259biological_processmethylation
A0046872molecular_functionmetal ion binding
A0102740molecular_functiontheobromine:S-adenosyl-L-methionine 1-N-methyltransferase activity
A0102741molecular_functionparaxanthine:S-adenosyl-L-methionine 3-N-methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE SAH A 501
ChainResidue
ALEU7
AGLY138
ASER139
APHE140
ATYR141
ACYS156
ATYR157
ACYS158
A37T502
AHOH510
AHOH517
AMET9
AHOH520
AHOH547
AHOH647
ATYR18
AGLY60
ACYS61
AALA62
AASN66
AASN99
AASP100

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 37T A 502
ChainResidue
ATYR18
ALEU26
APHE27
ATYR157
AHIS160
ATRP161
AILE226
ASER237
AILE332
ATYR368
ASAH501
AHOH509
AHOH587

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:17434991, ECO:0007744|PDB:2EFJ
ChainResidueDetails
ATYR18
AGLY60
AASN66
ALEU98
ASER139
ACYS156
ATYR157
ASER237
ATYR368

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A4GE69
ChainResidueDetails
AASN21
ATYR333

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A0A6C0WW36
ChainResidueDetails
ACYS61

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9FLN8
ChainResidueDetails
AASN178
AASP260
APHE262
AASN263

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Involved in substrate discrimination => ECO:0000250|UniProtKB:Q9FZN8
ChainResidueDetails
AHIS154
AILE266
AVAL328
AGLU343

223532

PDB entries from 2024-08-07

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