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4WKC

Crystal structure of Escherichia coli 5'-methylthioadenosine/S-adenosyl homocysteine nucleosidase (MTAN) complexed with butylthio-DADMe-Immucillin-A

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008782molecular_functionadenosylhomocysteine nucleosidase activity
A0008930molecular_functionmethylthioadenosine nucleosidase activity
A0009086biological_processmethionine biosynthetic process
A0009116biological_processnucleoside metabolic process
A0009164biological_processnucleoside catabolic process
A0016787molecular_functionhydrolase activity
A0019284biological_processL-methionine salvage from S-adenosylmethionine
A0019509biological_processL-methionine salvage from methylthioadenosine
A0046124biological_processpurine deoxyribonucleoside catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue BIG A 301
ChainResidue
AILE50
AGLU172
AMET173
AGLU174
ASER196
AASP197
APHE207
APG4302
APG4302
AHOH466
ASER76
AALA77
AGLY78
AVAL102
APHE105
AALA150
APHE151
AILE152

site_idAC2
Number of Residues9
Detailsbinding site for residue PG4 A 302
ChainResidue
AMET9
AMET9
AGLU11
AGLU11
APHE105
AASP208
AASP208
ABIG301
ABIG301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01684
ChainResidueDetails
AGLU12

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01684
ChainResidueDetails
AASP197

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01684
ChainResidueDetails
AGLY78
AILE152
AMET173

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PDB entries from 2024-07-24

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