7JID
Crystal structure of the L780 UDP-rhamnose synthase from Acanthamoeba polyphaga mimivirus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| A | 0008831 | molecular_function | dTDP-4-dehydrorhamnose reductase activity |
| A | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
| A | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
| A | 0048269 | cellular_component | methionine adenosyltransferase complex |
| A | 0048270 | molecular_function | methionine adenosyltransferase regulator activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| B | 0008831 | molecular_function | dTDP-4-dehydrorhamnose reductase activity |
| B | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
| B | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
| B | 0048269 | cellular_component | methionine adenosyltransferase complex |
| B | 0048270 | molecular_function | methionine adenosyltransferase regulator activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | binding site for residue AWU A 301 |
| Chain | Residue |
| A | THR59 |
| A | LYS175 |
| A | TYR179 |
| A | ARG181 |
| A | ILE182 |
| A | CYS183 |
| A | HIS221 |
| A | MET241 |
| A | GLN246 |
| A | ARG254 |
| A | NAP302 |
| A | THR66 |
| A | HOH423 |
| A | HOH504 |
| A | HOH537 |
| A | HOH545 |
| A | HOH546 |
| A | HOH560 |
| A | HOH564 |
| A | HOH569 |
| A | HOH623 |
| A | HOH658 |
| A | ILE67 |
| A | HOH666 |
| A | THR106 |
| A | CYS108 |
| A | TYR136 |
| A | ARG160 |
| A | MET161 |
| A | PRO162 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | binding site for residue NAP A 302 |
| Chain | Residue |
| A | GLY10 |
| A | TRP11 |
| A | ILE12 |
| A | ARG33 |
| A | ALA34 |
| A | ASP35 |
| A | PHE55 |
| A | ILE56 |
| A | GLY57 |
| A | ARG58 |
| A | HIS60 |
| A | ASP82 |
| A | LEU104 |
| A | AWU301 |
| A | HOH408 |
| A | HOH423 |
| A | HOH447 |
| A | HOH462 |
| A | HOH466 |
| A | HOH470 |
| A | HOH492 |
| A | HOH502 |
| A | HOH519 |
| A | HOH535 |
| A | HOH553 |
| A | HOH558 |
| A | HOH567 |
| A | HOH639 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | VAL198 |
| A | TYR268 |
| A | PRO269 |
| A | ASP270 |
| A | VAL271 |
| A | HOH495 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | GLU111 |
| A | GLY112 |
| A | ASN114 |
| A | ASN115 |
| A | ILE185 |
| A | ARG243 |
| A | ASN256 |
| A | HOH542 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 305 |
| Chain | Residue |
| A | GLU111 |
| A | GLN113 |
| A | PHE123 |
| A | HOH418 |
| A | HOH473 |
| A | HOH515 |
| A | HOH533 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 306 |
| Chain | Residue |
| A | THR237 |
| A | TRP238 |
| A | ASN240 |
| A | HOH584 |
| A | HOH588 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 307 |
| Chain | Residue |
| A | ILE176 |
| A | LEU177 |
| A | TYR179 |
| A | TRP238 |
| A | HOH410 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 308 |
| Chain | Residue |
| A | SER184 |
| A | ILE185 |
| A | SER242 |
| A | ARG243 |
| A | HOH436 |
| A | HOH565 |
| A | HOH649 |
| site_id | AC9 |
| Number of Residues | 28 |
| Details | binding site for residue AWU B 301 |
| Chain | Residue |
| B | THR106 |
| B | CYS108 |
| B | TYR136 |
| B | ARG160 |
| B | MET161 |
| B | PRO162 |
| B | PHE172 |
| B | LYS175 |
| B | TYR179 |
| B | ARG181 |
| B | ILE182 |
| B | CYS183 |
| B | HIS221 |
| B | MET241 |
| B | GLN246 |
| B | ARG254 |
| B | HOH413 |
| B | HOH422 |
| B | HOH440 |
| B | HOH498 |
| B | HOH499 |
| B | HOH524 |
| B | HOH549 |
| B | HOH567 |
| B | HOH571 |
| B | THR59 |
| B | THR66 |
| B | ILE67 |
| site_id | AD1 |
| Number of Residues | 25 |
| Details | binding site for residue NAP B 302 |
| Chain | Residue |
| B | LYS9 |
| B | GLY10 |
| B | TRP11 |
| B | ILE12 |
| B | ARG33 |
| B | ALA34 |
| B | ASP35 |
| B | PHE55 |
| B | ILE56 |
| B | GLY57 |
| B | ARG58 |
| B | THR59 |
| B | HIS60 |
| B | ASP82 |
| B | LEU104 |
| B | HOH421 |
| B | HOH455 |
| B | HOH467 |
| B | HOH473 |
| B | HOH479 |
| B | HOH507 |
| B | HOH513 |
| B | HOH537 |
| B | HOH568 |
| B | HOH576 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | PRO129 |
| B | ASN130 |
| B | HOH402 |
| B | HOH411 |
| site_id | AD3 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| B | PRO129 |
| B | PHE132 |
| B | VAL138 |
| B | GLY141 |
| B | PHE142 |
| B | ARG145 |
| B | HOH425 |
| B | HOH476 |
| B | HOH508 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 305 |
| Chain | Residue |
| B | LEU247 |
| B | LEU250 |
