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6AYO

Crystal structure of Campylobacter jejuni 5'-methylthioadenosine/S-adenosyl homocysteine nucleosidase (MTAN) complexed with 5'-deoxy-5'-Propyl-DADMe-Immucillin-A

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
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
B0008652biological_processamino acid biosynthetic process
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 C1Y A 301
ChainResidue
AALA8
AGLU171
AMET172
AGLU173
ASER195
AASP196
APHE206
AHOH414
AILE50
AVAL76
AALA77
AGLY78
AGLU150
APHE151
AILE152
ACYS170

site_idAC2
Number of Residues7
Detailsbinding site for residue EDO A 302
ChainResidue
AGLN97
AGLU116
AILE117
ALEU179
AHOH418
AHOH421
AHOH498

site_idAC3
Number of Residues16
Detailsbinding site for residue C1Y B 301
ChainResidue
BALA8
BILE50
BVAL76
BALA77
BGLY78
BGLU150
BPHE151
BILE152
BCYS170
BGLU171
BMET172
BGLU173
BSER195
BASP196
BPHE206
BHOH408

site_idAC4
Number of Residues8
Detailsbinding site for residue EDO B 302
ChainResidue
BGLN97
BGLU116
BILE117
BILE119
BLEU179
BHOH412
BHOH424
BHOH481

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO B 303
ChainResidue
BGLU116
BILE117
BPHE118
BEDO304
BHOH494

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO B 304
ChainResidue
BTYR47
BPHE111
BGLU116
BEDO303
BHOH490
BHOH520

site_idAC7
Number of Residues11
Detailsbinding site for residue BTB B 305
ChainResidue
AGLY114
BGLU27
BASN30
BASN31
BTHR32
BTYR47
BLYS49
BGLY114
BASN115
BHOH439
BHOH466

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AGLU12
BGLU12

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AASP196
BASP196

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AMET172
BGLY78
BILE152
BMET172
AGLY78
AILE152

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PDB entries from 2024-04-17

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