3DP9
Crystal structure of Vibrio cholerae 5'-methylthioadenosine/S-adenosyl homocysteine nucleosidase (MTAN) complexed with butylthio-DADMe-Immucillin A
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 | 0016787 | molecular_function | hydrolase activity |
A | 0019284 | biological_process | L-methionine salvage from S-adenosylmethionine |
A | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
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 | 0016787 | molecular_function | hydrolase activity |
C | 0019284 | biological_process | L-methionine salvage from S-adenosylmethionine |
C | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IOD C 300 |
Chain | Residue |
A | THR139 |
C | PRO137 |
C | THR139 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE BIG A 301 |
Chain | Residue |
A | VAL153 |
A | VAL172 |
A | GLU173 |
A | MET174 |
A | GLU175 |
A | SER197 |
A | ASP198 |
A | PHE208 |
A | HOH305 |
C | PHE105 |
A | ILE50 |
A | SER76 |
A | ALA77 |
A | GLY78 |
A | ALA151 |
A | PHE152 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE BIG C 301 |
Chain | Residue |
C | ILE50 |
C | SER76 |
C | ALA77 |
C | GLY78 |
C | ALA151 |
C | PHE152 |
C | VAL153 |
C | VAL172 |
C | GLU173 |
C | MET174 |
C | GLU175 |
C | SER197 |
C | ASP198 |
C | PHE208 |
C | HOH302 |
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 | |
C | 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 | |
C | 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 | |
C | GLY78 | |
C | VAL153 | |
C | MET174 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a69 |
Chain | Residue | Details |
A | PHE211 | |
A | ASP198 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a69 |
Chain | Residue | Details |
C | PHE211 | |
C | ASP198 |