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
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005829 | cellular_component | cytosol |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0008782 | molecular_function | adenosylhomocysteine nucleosidase activity |
A | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
A | 0009086 | biological_process | methionine biosynthetic process |
A | 0009116 | biological_process | nucleoside metabolic process |
A | 0009164 | biological_process | nucleoside catabolic process |
A | 0009234 | biological_process | menaquinone biosynthetic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019284 | biological_process | L-methionine salvage from S-adenosylmethionine |
A | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
A | 0102246 | molecular_function | 6-amino-6-deoxyfutalosine hydrolase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0005829 | cellular_component | cytosol |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0008782 | molecular_function | adenosylhomocysteine nucleosidase activity |
B | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
B | 0009086 | biological_process | methionine biosynthetic process |
B | 0009116 | biological_process | nucleoside metabolic process |
B | 0009164 | biological_process | nucleoside catabolic process |
B | 0009234 | biological_process | menaquinone biosynthetic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0019284 | biological_process | L-methionine salvage from S-adenosylmethionine |
B | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
B | 0102246 | molecular_function | 6-amino-6-deoxyfutalosine hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | binding site for residue C1Y A 301 |
Chain | Residue |
A | ALA8 |
A | GLU171 |
A | MET172 |
A | GLU173 |
A | SER195 |
A | ASP196 |
A | PHE206 |
A | HOH414 |
A | ILE50 |
A | VAL76 |
A | ALA77 |
A | GLY78 |
A | GLU150 |
A | PHE151 |
A | ILE152 |
A | CYS170 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
A | GLN97 |
A | GLU116 |
A | ILE117 |
A | LEU179 |
A | HOH418 |
A | HOH421 |
A | HOH498 |
site_id | AC3 |
Number of Residues | 16 |
Details | binding site for residue C1Y B 301 |
Chain | Residue |
B | ALA8 |
B | ILE50 |
B | VAL76 |
B | ALA77 |
B | GLY78 |
B | GLU150 |
B | PHE151 |
B | ILE152 |
B | CYS170 |
B | GLU171 |
B | MET172 |
B | GLU173 |
B | SER195 |
B | ASP196 |
B | PHE206 |
B | HOH408 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue EDO B 302 |
Chain | Residue |
B | GLN97 |
B | GLU116 |
B | ILE117 |
B | ILE119 |
B | LEU179 |
B | HOH412 |
B | HOH424 |
B | HOH481 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
B | GLU116 |
B | ILE117 |
B | PHE118 |
B | EDO304 |
B | HOH494 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO B 304 |
Chain | Residue |
B | TYR47 |
B | PHE111 |
B | GLU116 |
B | EDO303 |
B | HOH490 |
B | HOH520 |
site_id | AC7 |
Number of Residues | 11 |
Details | binding site for residue BTB B 305 |
Chain | Residue |
A | GLY114 |
B | GLU27 |
B | ASN30 |
B | ASN31 |
B | THR32 |
B | TYR47 |
B | LYS49 |
B | GLY114 |
B | ASN115 |
B | HOH439 |
B | HOH466 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | GLU12 | |
B | GLU12 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000250 |
Chain | Residue | Details |
A | ASP196 | |
B | ASP196 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | MET172 | |
B | GLY78 | |
B | ILE152 | |
B | MET172 | |
A | GLY78 | |
A | ILE152 |