6DYY
Crystal structure of Helicobacter pylori 5'-methylthioadenosine/S-adenosyl homocysteine nucleosidase (MTAN) complexed with (3R,4S)-1-((4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl)-4-(((3-(1-butyl-1H-1,2,3-triazol-4-yl)propyl)thio)methyl)pyrrolidin-3-ol
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005829 | cellular_component | cytosol |
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 | 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 |
C | 0003824 | molecular_function | catalytic activity |
C | 0005829 | cellular_component | cytosol |
C | 0008782 | molecular_function | adenosylhomocysteine nucleosidase activity |
C | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
C | 0009086 | biological_process | methionine biosynthetic process |
C | 0009116 | biological_process | nucleoside metabolic process |
C | 0009164 | biological_process | nucleoside catabolic process |
C | 0009234 | biological_process | menaquinone biosynthetic process |
C | 0016787 | molecular_function | hydrolase activity |
C | 0019284 | biological_process | L-methionine salvage from S-adenosylmethionine |
C | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
C | 0102246 | molecular_function | 6-amino-6-deoxyfutalosine hydrolase activity |
D | 0003824 | molecular_function | catalytic activity |
D | 0005829 | cellular_component | cytosol |
D | 0008782 | molecular_function | adenosylhomocysteine nucleosidase activity |
D | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
D | 0009086 | biological_process | methionine biosynthetic process |
D | 0009116 | biological_process | nucleoside metabolic process |
D | 0009164 | biological_process | nucleoside catabolic process |
D | 0009234 | biological_process | menaquinone biosynthetic process |
D | 0016787 | molecular_function | hydrolase activity |
D | 0019284 | biological_process | L-methionine salvage from S-adenosylmethionine |
D | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
D | 0102246 | molecular_function | 6-amino-6-deoxyfutalosine hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue EDO A 301 |
Chain | Residue |
A | THR123 |
A | GLY125 |
A | SER126 |
A | HOH464 |
C | ASP209 |
D | PHE107 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue MG A 302 |
Chain | Residue |
A | HOH418 |
A | HOH428 |
A | HOH579 |
A | HOH591 |
A | GLU229 |
A | HOH401 |
A | HOH403 |
site_id | AC3 |
Number of Residues | 19 |
Details | binding site for residue OS6 A 303 |
Chain | Residue |
A | ILE52 |
A | VAL78 |
A | ALA79 |
A | GLY80 |
A | GLN152 |
A | PHE153 |
A | VAL154 |
A | VAL172 |
A | GLU173 |
A | MET174 |
A | GLU175 |
A | SER197 |
A | ASP198 |
A | ALA200 |
A | PHE208 |
A | HOH416 |
B | HIS109 |
B | PRO115 |
B | GLU116 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue EDO B 301 |
Chain | Residue |
B | THR123 |
B | GLY125 |
B | SER126 |
B | HOH403 |
B | HOH562 |
C | PHE107 |
D | ASP209 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue EDO B 302 |
Chain | Residue |
A | ALA106 |
A | PHE107 |
B | GLY205 |
B | MET206 |
B | ASP209 |
B | HOH457 |
B | HOH492 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
B | GLN138 |
B | HIS139 |
B | SER165 |
B | GLU166 |
B | HOH536 |
B | HOH546 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue MG B 304 |
Chain | Residue |
B | LYS133 |
B | HOH401 |
B | HOH411 |
B | HOH424 |
B | HOH453 |
B | HOH585 |
B | HOH601 |
site_id | AC8 |
Number of Residues | 21 |
Details | binding site for residue OS6 B 305 |
Chain | Residue |
A | LEU104 |
A | HIS109 |
A | PRO115 |
B | ALA9 |
B | ILE52 |
B | VAL78 |
B | ALA79 |
B | GLY80 |
B | GLN152 |
B | PHE153 |
B | VAL154 |
B | VAL172 |
B | GLU173 |
B | MET174 |
B | GLU175 |
B | SER197 |
B | ASP198 |
B | PHE208 |
B | HOH423 |
C | LYS132 |
C | HOH483 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue EDO C 301 |
Chain | Residue |
C | GLY32 |
C | ASN33 |
C | VAL34 |
C | TYR49 |
C | HOH478 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue EDO C 302 |
Chain | Residue |
A | LYS157 |
C | SER156 |
C | LYS157 |
C | ASP201 |
C | GLU202 |
C | HOH413 |
site_id | AD2 |
Number of Residues | 19 |
Details | binding site for residue OS6 C 303 |
Chain | Residue |
C | VAL154 |
C | VAL172 |
C | GLU173 |
C | MET174 |
C | GLU175 |
C | SER197 |
C | ASP198 |
C | PHE208 |
C | HOH417 |
D | PHE107 |
D | HIS109 |
A | GLU122 |
C | ALA9 |
C | ILE52 |
C | VAL78 |
C | ALA79 |
C | GLY80 |
C | GLN152 |
C | PHE153 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue EDO D 301 |
Chain | Residue |
D | GLY32 |
D | ASN33 |
D | VAL34 |
D | TYR49 |
D | HOH446 |
site_id | AD4 |
Number of Residues | 16 |
Details | binding site for residue OS6 D 302 |
Chain | Residue |
C | HIS109 |
D | ALA9 |
D | ILE52 |
D | VAL78 |
D | ALA79 |
D | GLY80 |
D | PHE153 |
D | VAL154 |
D | VAL172 |
D | GLU173 |
D | MET174 |
D | GLU175 |
D | SER197 |
D | ASP198 |
D | PHE208 |
D | HOH410 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:20954236 |
Chain | Residue | Details |
A | GLU13 | |
B | GLU13 | |
C | GLU13 | |
D | GLU13 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:20954236 |
Chain | Residue | Details |
A | ASP198 | |
B | ASP198 | |
C | ASP198 | |
D | ASP198 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
D | GLY80 | |
A | GLY80 | |
B | GLY80 | |
C | GLY80 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
C | VAL154 | |
C | MET174 | |
D | VAL154 | |
D | MET174 | |
A | VAL154 | |
A | MET174 | |
B | VAL154 | |
B | MET174 |