3MBO
Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0071793 | biological_process | bacillithiol biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0071793 | biological_process | bacillithiol biosynthetic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0071793 | biological_process | bacillithiol biosynthetic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0071793 | biological_process | bacillithiol biosynthetic process |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0016740 | molecular_function | transferase activity |
| E | 0016757 | molecular_function | glycosyltransferase activity |
| E | 0071793 | biological_process | bacillithiol biosynthetic process |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0016740 | molecular_function | transferase activity |
| F | 0016757 | molecular_function | glycosyltransferase activity |
| F | 0071793 | biological_process | bacillithiol biosynthetic process |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0016740 | molecular_function | transferase activity |
| G | 0016757 | molecular_function | glycosyltransferase activity |
| G | 0071793 | biological_process | bacillithiol biosynthetic process |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0016740 | molecular_function | transferase activity |
| H | 0016757 | molecular_function | glycosyltransferase activity |
| H | 0071793 | biological_process | bacillithiol biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE UDP A 382 |
| Chain | Residue |
| A | VAL13 |
| A | GLY285 |
| A | LEU286 |
| A | GLU290 |
| A | GOL386 |
| A | GLY14 |
| A | GLY15 |
| A | ILE204 |
| A | ASN206 |
| A | LYS211 |
| A | VAL234 |
| A | GLN262 |
| A | GLU282 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE UDP C 382 |
| Chain | Residue |
| C | GLY15 |
| C | ILE204 |
| C | LYS211 |
| C | LYS261 |
| C | GLN262 |
| C | GLU282 |
| C | GLY285 |
| C | LEU286 |
| C | VAL287 |
| C | GLU290 |
| C | GOL383 |
| C | MLT385 |
| C | MG386 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE UDP H 382 |
| Chain | Residue |
| H | GLY15 |
| H | ILE204 |
| H | SER205 |
| H | ASN206 |
| H | GLY235 |
| H | ASP236 |
| H | LEU286 |
| H | GLU290 |
| H | MLT384 |
| H | HOH427 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE UDP E 382 |
| Chain | Residue |
| E | GLY15 |
| E | ILE204 |
| E | SER205 |
| E | ASN206 |
| E | LYS211 |
| E | GLN262 |
| E | ASP263 |
| E | ASN264 |
| E | VAL265 |
| E | GLY285 |
| E | LEU286 |
| E | GLU290 |
| E | GOL384 |
| E | MLT387 |
| E | MG388 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 383 |
| Chain | Residue |
| A | ARG138 |
| A | GLU142 |
| A | LYS163 |
| A | ASN165 |
| D | ASN165 |
| D | ASP167 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL F 382 |
| Chain | Residue |
| F | LYS182 |
| F | ARG183 |
| F | LEU269 |
| F | ALA270 |
| F | SER272 |
| F | CYS294 |
| F | GLY295 |
| F | VAL296 |
| F | HIS341 |
| F | HOH399 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL F 383 |
| Chain | Residue |
| F | ASN46 |
| F | LYS47 |
| F | TYR49 |
| F | ILE52 |
| F | PHE54 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL E 383 |
| Chain | Residue |
| E | GLY313 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL F 384 |
| Chain | Residue |
| E | TYR67 |
| E | PRO68 |
| F | PRO68 |
| F | TYR70 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 382 |
| Chain | Residue |
| D | VAL59 |
| D | ASN60 |
| D | VAL64 |
| D | GLN66 |
| D | PRO69 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL H 383 |
| Chain | Residue |
| H | LYS2 |
| H | TYR370 |
| H | ARG374 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 384 |
| Chain | Residue |
| A | THR367 |
| A | TYR370 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 382 |
| Chain | Residue |
| B | THR125 |
| B | SER153 |
| B | GLU157 |
| B | LYS281 |
| B | GLU282 |
| B | GLY304 |
| B | GOL383 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 383 |
| Chain | Residue |
| D | ALA221 |
| D | THR225 |
| D | LEU250 |
| D | HIS251 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL D 384 |
| Chain | Residue |
| D | HIS251 |
| D | ASN249 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 385 |
| Chain | Residue |
| A | GLN169 |
| A | THR170 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 386 |
| Chain | Residue |
| A | GLY121 |
| A | THR122 |
| A | THR125 |
| A | GLU282 |
| A | SER283 |
| A | UDP382 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 383 |
| Chain | Residue |
| B | GLU157 |
| B | GOL382 |
| site_id | CC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL E 384 |
| Chain | Residue |
| E | VAL179 |
| E | TYR180 |
| E | ASN264 |
| E | VAL265 |
| E | ALA266 |
| E | GLU290 |
| E | UDP382 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 383 |
| Chain | Residue |
| C | PHE43 |
| C | TYR180 |
| C | VAL265 |
| C | GLU290 |
| C | UDP382 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 387 |
| Chain | Residue |
| A | GLU354 |
| A | GLN355 |
| A | LYS360 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL E 385 |
| Chain | Residue |
| E | LYS182 |
| E | CYS294 |
| E | GLY295 |
| E | GLY345 |
| E | ARG349 |
| G | ASP236 |
| site_id | CC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 384 |
| Chain | Residue |
| C | SER363 |
| C | GLN364 |
| C | THR367 |
| site_id | CC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL F 385 |
| Chain | Residue |
| F | GLY121 |
| F | GLU282 |
| F | SER283 |
| F | PHE284 |
| F | GLY285 |
| site_id | CC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL E 386 |
| Chain | Residue |
| E | ASP145 |
| E | VAL146 |
| E | VAL147 |
| E | LYS166 |
| E | ASP167 |
| site_id | CC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MLT H 384 |
| Chain | Residue |
| H | GLY14 |
| H | GLY15 |
| H | SER16 |
| H | TYR94 |
| H | THR122 |
| H | ASN206 |
| H | UDP382 |
| site_id | CC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MLT A 388 |
| Chain | Residue |
| A | TYR10 |
| A | SER16 |
| A | TYR94 |
| A | THR122 |
| B | VAL64 |
| site_id | DC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MLT C 385 |
| Chain | Residue |
| C | VAL13 |
| C | GLY14 |
| C | GLY15 |
| C | SER16 |
| C | TYR94 |
| C | THR122 |
| C | UDP382 |
| C | HOH397 |
| site_id | DC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MLT E 387 |
| Chain | Residue |
| E | GLY14 |
| E | GLY15 |
| E | SER16 |
| E | THR122 |
| E | ASN206 |
| E | UDP382 |
| F | PHE65 |
| site_id | DC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 386 |
| Chain | Residue |
| C | GLU282 |
| C | GLY285 |
| C | UDP382 |
| site_id | DC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG E 388 |
| Chain | Residue |
| E | GLU282 |
| E | PHE284 |
| E | UDP382 |
| E | HOH400 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20799687","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3MBO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |






