3LGS
A. thaliana MTA nucleosidase in complex with S-adenosylhomocysteine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000003 | biological_process | obsolete reproduction |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0009116 | biological_process | nucleoside metabolic process |
| A | 0010087 | biological_process | phloem or xylem histogenesis |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| B | 0000003 | biological_process | obsolete reproduction |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0009116 | biological_process | nucleoside metabolic process |
| B | 0010087 | biological_process | phloem or xylem histogenesis |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| C | 0000003 | biological_process | obsolete reproduction |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
| C | 0009086 | biological_process | methionine biosynthetic process |
| C | 0009116 | biological_process | nucleoside metabolic process |
| C | 0010087 | biological_process | phloem or xylem histogenesis |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| D | 0000003 | biological_process | obsolete reproduction |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
| D | 0009086 | biological_process | methionine biosynthetic process |
| D | 0009116 | biological_process | nucleoside metabolic process |
| D | 0010087 | biological_process | phloem or xylem histogenesis |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE SAH A 268 |
| Chain | Residue |
| A | VAL90 |
| A | THR224 |
| A | ASP225 |
| A | THR233 |
| A | PHE237 |
| A | HOH414 |
| A | HOH518 |
| A | HOH520 |
| A | HOH525 |
| A | THR116 |
| A | CYS117 |
| A | GLY118 |
| A | LEU181 |
| A | LYS199 |
| A | ASP200 |
| A | MET201 |
| A | GLU202 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADE A 269 |
| Chain | Residue |
| A | CYS117 |
| A | GLY118 |
| A | LEU181 |
| A | LYS199 |
| A | ASP200 |
| A | MET201 |
| A | THR224 |
| A | ASP225 |
| A | VAL227 |
| A | THR233 |
| A | HOH301 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 2638 |
| Chain | Residue |
| A | ALA37 |
| A | PRO41 |
| A | THR242 |
| A | HOH312 |
| A | HOH360 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 270 |
| Chain | Residue |
| A | VAL153 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE SAH B 268 |
| Chain | Residue |
| B | THR116 |
| B | CYS117 |
| B | GLY118 |
| B | LEU181 |
| B | LYS199 |
| B | ASP200 |
| B | MET201 |
| B | GLU202 |
| B | THR224 |
| B | ASP225 |
| B | THR233 |
| B | PHE237 |
| B | HOH305 |
| B | HOH517 |
| B | HOH523 |
| B | HOH527 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADE B 269 |
| Chain | Residue |
| B | CYS117 |
| B | GLY118 |
| B | LEU181 |
| B | LYS199 |
| B | ASP200 |
| B | MET201 |
| B | THR224 |
| B | ASP225 |
| B | VAL227 |
| B | PHE237 |
| B | HOH289 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 2638 |
| Chain | Residue |
| B | VAL130 |
| B | LEU170 |
| B | LYS171 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO B 270 |
| Chain | Residue |
| B | GLU167 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 271 |
| Chain | Residue |
| B | ALA207 |
| B | ALA210 |
| B | ASP211 |
| B | ILE215 |
| B | VAL217 |
| B | HOH351 |
| B | HOH403 |
| site_id | BC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SAH C 268 |
| Chain | Residue |
| C | THR116 |
| C | CYS117 |
| C | GLY118 |
| C | LEU181 |
| C | LYS199 |
| C | ASP200 |
| C | MET201 |
| C | GLU202 |
| C | THR224 |
| C | ASP225 |
| C | THR233 |
| C | PHE237 |
| C | HOH494 |
| C | HOH516 |
| C | HOH521 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADE C 269 |
| Chain | Residue |
| C | CYS117 |
| C | GLY118 |
| C | LEU181 |
| C | LYS199 |
| C | ASP200 |
| C | MET201 |
| C | THR224 |
| C | ASP225 |
| C | VAL227 |
| C | THR233 |
| C | PHE237 |
| C | HOH289 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 2638 |
| Chain | Residue |
| C | VAL153 |
| C | ARG174 |
| C | ASN194 |
| C | HOH307 |
| site_id | BC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE SAH D 268 |
| Chain | Residue |
| D | VAL90 |
| D | THR116 |
| D | CYS117 |
| D | GLY118 |
| D | LEU181 |
| D | LYS199 |
| D | ASP200 |
| D | MET201 |
| D | THR224 |
| D | ASP225 |
| D | THR233 |
| D | PHE237 |
| D | HOH355 |
| D | HOH519 |
| D | HOH524 |
| D | HOH526 |
| site_id | BC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADE D 269 |
| Chain | Residue |
| D | CYS117 |
| D | GLY118 |
| D | LEU181 |
| D | LYS199 |
| D | ASP200 |
| D | MET201 |
| D | THR224 |
| D | ASP225 |
| D | THR233 |
| D | PHE237 |
| D | HOH287 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO D 2638 |
| Chain | Residue |
| D | VAL130 |
| D | LEU170 |
| D | LYS171 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 270 |
| Chain | Residue |
| D | SER54 |
| D | PRO55 |
| D | LEU56 |
| D | TRP62 |
| D | LEU64 |
| D | HOH275 |
| D | HOH284 |
| D | HOH306 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO D 271 |
| Chain | Residue |
| D | SER134 |
| D | ALA158 |
| D | THR161 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:20554051 |
| Chain | Residue | Details |
| A | GLU38 | |
| B | GLU38 | |
| C | GLU38 | |
| D | GLU38 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:20554051 |
| Chain | Residue | Details |
| A | ASP225 | |
| B | ASP225 | |
| C | ASP225 | |
| D | ASP225 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:18342331, ECO:0000305|PubMed:20554051, ECO:0007744|PDB:2QTT, ECO:0007744|PDB:3LGS |
| Chain | Residue | Details |
| A | THR116 | |
| A | ASP225 | |
| B | THR116 | |
| B | ASP225 | |
| C | THR116 | |
| C | ASP225 | |
| D | THR116 | |
| D | ASP225 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16909418, ECO:0000269|PubMed:20554051, ECO:0007744|PDB:2H8G, ECO:0007744|PDB:3LGS |
| Chain | Residue | Details |
| A | LYS199 | |
| B | LYS199 | |
| C | LYS199 | |
| D | LYS199 |
