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1NC3

Crystal structure of E. coli MTA/AdoHcy nucleosidase complexed with formycin A (FMA)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
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
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046124biological_processpurine deoxyribonucleoside catabolic process
A0110052biological_processtoxic metabolite repair
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0008782molecular_functionadenosylhomocysteine nucleosidase activity
B0008930molecular_functionmethylthioadenosine nucleosidase activity
B0009086biological_processmethionine biosynthetic process
B0009116biological_processnucleoside metabolic process
B0009164biological_processnucleoside catabolic process
B0016787molecular_functionhydrolase activity
B0019284biological_processL-methionine salvage from S-adenosylmethionine
B0019509biological_processL-methionine salvage from methylthioadenosine
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046124biological_processpurine deoxyribonucleoside catabolic process
B0110052biological_processtoxic metabolite repair
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE FMC A 233
ChainResidue
ASER76
AARG193
ASER196
AASP197
AALA199
APHE207
AHOH236
AALA77
AGLY78
AALA150
APHE151
AILE152
AGLU172
AMET173
AGLU174

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE FMC B 234
ChainResidue
BALA8
BSER76
BALA77
BGLY78
BALA150
BPHE151
BILE152
BGLU172
BMET173
BGLU174
BARG193
BSER196
BASP197
BALA199
BPHE207
BHOH241

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01684, ECO:0000305|PubMed:16109423
ChainResidueDetails
BGLU12
AGLU12

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01684, ECO:0000305|PubMed:16109423
ChainResidueDetails
BASP197
AASP197

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01684, ECO:0000269|PubMed:11591349
ChainResidueDetails
AGLY78
BGLY78
BILE152
AILE152

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01684
ChainResidueDetails
AMET173
BMET173

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PDB entries from 2024-06-12

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