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3NM5

Helicobacter pylori MTAN complexed with Formycin A

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
A0009234biological_processmenaquinone biosynthetic process
A0016787molecular_functionhydrolase activity
A0019284biological_processL-methionine salvage from S-adenosylmethionine
A0019509biological_processL-methionine salvage from methylthioadenosine
A0102246molecular_function6-amino-6-deoxyfutalosine hydrolase activity
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
B0009234biological_processmenaquinone biosynthetic process
B0016787molecular_functionhydrolase activity
B0019284biological_processL-methionine salvage from S-adenosylmethionine
B0019509biological_processL-methionine salvage from methylthioadenosine
B0102246molecular_function6-amino-6-deoxyfutalosine hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE FMC A 501
ChainResidue
AALA9
AGLU175
AARG194
ASER197
AASP198
APHE208
AHOH328
BLEU104
AVAL78
AALA79
AGLY80
AGLN152
APHE153
AVAL154
AGLU173
AMET174

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE FMC B 502
ChainResidue
BALA9
BILE52
BVAL78
BGLY80
BGLN152
BPHE153
BVAL154
BGLU173
BMET174
BGLU175
BARG194
BASP198
BPHE208
BHOH293

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:20954236
ChainResidueDetails
AGLU13
BGLU13

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:20954236
ChainResidueDetails
AASP198
BASP198

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY80
BGLY80

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AVAL154
BVAL154
BMET174
AMET174

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PDB entries from 2024-05-15

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