5UE1
Crystal structure of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase in complex with adenine from Vibrio fischeri ES114
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
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 | 0016787 | molecular_function | hydrolase activity |
A | 0019284 | biological_process | L-methionine salvage from S-adenosylmethionine |
A | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
B | 0003824 | molecular_function | catalytic activity |
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 | 0016787 | molecular_function | hydrolase activity |
B | 0019284 | biological_process | L-methionine salvage from S-adenosylmethionine |
B | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | binding site for residue 9DA A 301 |
Chain | Residue |
A | ALA77 |
A | TRS302 |
A | GLY78 |
A | VAL151 |
A | PHE152 |
A | VAL153 |
A | GLU173 |
A | SER197 |
A | ASP198 |
A | ALA200 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue TRS A 302 |
Chain | Residue |
A | MET9 |
A | GLU12 |
A | SER76 |
A | PHE152 |
A | GLU173 |
A | MET174 |
A | GLU175 |
A | ARG194 |
A | PHE208 |
A | 9DA301 |
A | HOH516 |
B | EDO306 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue CA A 303 |
Chain | Residue |
A | ASN-1 |
A | HOH597 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue CA A 304 |
Chain | Residue |
A | ASP18 |
A | HOH559 |
A | HOH647 |
B | ASP18 |
B | HOH549 |
B | HOH609 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue CA A 305 |
Chain | Residue |
A | MET206 |
A | ASP209 |
A | GLU210 |
A | HOH598 |
A | HOH609 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue CL A 306 |
Chain | Residue |
A | MET9 |
A | GLU10 |
A | GLN11 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue CL A 307 |
Chain | Residue |
A | VAL142 |
A | ARG143 |
site_id | AC8 |
Number of Residues | 10 |
Details | binding site for residue 9DA B 301 |
Chain | Residue |
B | ALA77 |
B | GLY78 |
B | VAL151 |
B | PHE152 |
B | VAL153 |
B | GLU173 |
B | SER197 |
B | ASP198 |
B | ALA200 |
B | TRS302 |
site_id | AC9 |
Number of Residues | 12 |
Details | binding site for residue TRS B 302 |
Chain | Residue |
B | ALA8 |
B | MET9 |
B | GLU12 |
B | SER76 |
B | PHE152 |
B | GLU173 |
B | MET174 |
B | GLU175 |
B | ARG194 |
B | PHE208 |
B | 9DA301 |
B | HOH486 |
site_id | AD1 |
Number of Residues | 7 |
Details | binding site for residue CL B 303 |
Chain | Residue |
A | MET112 |
A | GLN181 |
B | ILE50 |
B | GLY51 |
B | VAL53 |
B | ALA54 |
B | HOH463 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue CL B 304 |
Chain | Residue |
B | GLU10 |
B | GLN11 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue CL B 305 |
Chain | Residue |
B | VAL142 |
B | ARG143 |
B | HOH464 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue EDO B 306 |
Chain | Residue |
A | TRS302 |
B | PHE105 |
B | HOH451 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01684 |
Chain | Residue | Details |
A | GLU12 | |
B | GLU12 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01684 |
Chain | Residue | Details |
A | ASP198 | |
B | ASP198 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01684 |
Chain | Residue | Details |
A | GLY78 | |
A | VAL153 | |
A | MET174 | |
B | GLY78 | |
B | VAL153 | |
B | MET174 |