3HDQ
Crystal structure of UDP-galactopyranose mutase (oxidized form) in complex with substrate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0005829 | cellular_component | cytosol |
| E | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
| E | 0016853 | molecular_function | isomerase activity |
| E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0005829 | cellular_component | cytosol |
| F | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
| F | 0016853 | molecular_function | isomerase activity |
| F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0005829 | cellular_component | cytosol |
| G | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
| G | 0016853 | molecular_function | isomerase activity |
| G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0005829 | cellular_component | cytosol |
| H | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
| H | 0016853 | molecular_function | isomerase activity |
| H | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| I | 0000166 | molecular_function | nucleotide binding |
| I | 0005829 | cellular_component | cytosol |
| I | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
| I | 0016853 | molecular_function | isomerase activity |
| I | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| J | 0000166 | molecular_function | nucleotide binding |
| J | 0005829 | cellular_component | cytosol |
| J | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
| J | 0016853 | molecular_function | isomerase activity |
| J | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE GDU A 500 |
| Chain | Residue |
| A | HIS109 |
| A | TYR209 |
| A | PHE210 |
| A | THR294 |
| A | ASN296 |
| A | ARG305 |
| A | TYR335 |
| A | TYR370 |
| A | HOH412 |
| A | HOH440 |
| A | HOH441 |
| A | PHE175 |
| A | HOH448 |
| A | FAD450 |
| A | HOH644 |
| A | HOH1224 |
| A | HOH1234 |
| A | HOH1235 |
| A | PHE176 |
| A | TYR179 |
| A | THR180 |
| A | TRP184 |
| A | VAL195 |
| A | ARG198 |
| A | VAL199 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD A 450 |
| Chain | Residue |
| A | VAL35 |
| A | GLY36 |
| A | GLY38 |
| A | PHE39 |
| A | ALA40 |
| A | ASP59 |
| A | ARG60 |
| A | ARG61 |
| A | GLY66 |
| A | ASN67 |
| A | TYR82 |
| A | PRO84 |
| A | HIS85 |
| A | ILE86 |
| A | THR241 |
| A | ASP242 |
| A | TYR243 |
| A | THR258 |
| A | GLY259 |
| A | LEU277 |
| A | GLY363 |
| A | ARG364 |
| A | TYR371 |
| A | ASN372 |
| A | MET373 |
| A | VAL376 |
| A | HOH399 |
| A | HOH402 |
| A | HOH408 |
| A | HOH420 |
| A | HOH463 |
| A | GDU500 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE GDU B 500 |
| Chain | Residue |
| B | ILE86 |
| B | HIS109 |
| B | PHE175 |
| B | PHE176 |
| B | TYR179 |
| B | THR180 |
| B | TRP184 |
| B | VAL195 |
| B | ARG198 |
| B | VAL199 |
| B | TYR209 |
| B | PHE210 |
| B | THR294 |
| B | ASN296 |
| B | ARG305 |
| B | TYR335 |
| B | TYR370 |
| B | HOH421 |
| B | FAD450 |
| B | HOH933 |
| B | HOH980 |
| B | HOH1236 |
| B | HOH1237 |
| site_id | AC4 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD B 450 |
| Chain | Residue |
| B | GLY363 |
| B | ARG364 |
| B | TYR371 |
| B | ASN372 |
| B | MET373 |
| B | VAL376 |
| B | HOH411 |
| B | HOH420 |
| B | HOH427 |
| B | GDU500 |
| B | HOH905 |
| B | GLY36 |
| B | GLY38 |
| B | PHE39 |
| B | ALA40 |
| B | ASP59 |
| B | ARG60 |
| B | ARG61 |
| B | GLY66 |
| B | ASN67 |
| B | TYR82 |
| B | PRO84 |
| B | HIS85 |
| B | ILE86 |
| B | THR241 |
| B | ASP242 |
| B | TYR243 |
| B | LEU277 |
| B | TYR334 |
| B | TYR335 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE GDU C 500 |
| Chain | Residue |
| C | ILE86 |
| C | HIS109 |
| C | PHE175 |
| C | PHE176 |
| C | TYR179 |
| C | THR180 |
| C | TRP184 |
| C | VAL195 |
| C | ARG198 |
| C | VAL199 |
| C | TYR209 |
| C | PHE210 |
| C | THR294 |
| C | ASN296 |
| C | ARG305 |
| C | TYR335 |
| C | TYR370 |
| C | HOH419 |
| C | FAD450 |
| C | HOH1007 |
| C | HOH1238 |
| site_id | AC6 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD C 450 |
| Chain | Residue |
| C | GLY36 |
| C | GLY38 |
| C | PHE39 |
| C | ALA40 |
| C | ASP59 |
| C | ARG60 |
| C | ARG61 |
| C | GLY66 |
| C | ASN67 |
| C | PRO84 |
| C | HIS85 |
| C | ILE86 |
| C | HIS88 |
| C | THR241 |
| C | ASP242 |
| C | TYR243 |
| C | THR258 |
| C | LEU277 |
| C | TYR334 |
| C | GLY363 |
| C | ARG364 |
| C | TYR371 |
| C | ASN372 |
| C | MET373 |
| C | HOH412 |
| C | GDU500 |
| C | HOH536 |
| C | HOH990 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE GDU D 500 |
| Chain | Residue |
| D | HIS109 |
| D | VAL111 |
| D | PHE175 |
| D | PHE176 |
| D | TYR179 |
| D | THR180 |
| D | TRP184 |
| D | VAL195 |
| D | ARG198 |
| D | VAL199 |
| D | TYR209 |
| D | PHE210 |
| D | THR294 |
| D | ASN296 |
| D | ARG305 |
| D | TYR335 |
| D | TYR370 |
| D | FAD450 |
| D | HOH530 |
| D | HOH1030 |
| D | HOH1239 |
| D | HOH1240 |
| D | HOH1241 |
| site_id | AC8 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD D 450 |
| Chain | Residue |
| D | VAL35 |
| D | GLY36 |
| D | GLY38 |
| D | PHE39 |
| D | ALA40 |
| D | ASP59 |
| D | ARG60 |
| D | ARG61 |
| D | GLY66 |
| D | ASN67 |
| D | TYR82 |
| D | PRO84 |
| D | HIS85 |
| D | ILE86 |
| D | THR241 |
| D | ASP242 |
| D | TYR243 |
| D | GLY259 |
| D | TYR334 |
| D | TYR335 |
| D | GLY363 |
| D | ARG364 |
| D | TYR371 |
| D | ASN372 |
| D | MET373 |
| D | VAL376 |
| D | HOH410 |
| D | HOH412 |
| D | HOH414 |
| D | GDU500 |
| D | HOH1033 |
| site_id | AC9 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE GDU E 500 |
| Chain | Residue |
| E | ILE86 |
| E | HIS109 |
| E | VAL111 |
| E | ILE122 |
| E | PHE175 |
| E | PHE176 |
| E | TYR179 |
| E | THR180 |
| E | TRP184 |
| E | VAL195 |
| E | ARG198 |
| E | VAL199 |
| E | TYR209 |
| E | PHE210 |
| E | THR294 |
| E | ASN296 |
| E | ARG305 |
| E | TYR335 |
| E | TYR370 |
| E | FAD450 |
| E | HOH567 |
| E | HOH616 |
| E | HOH660 |
| E | HOH1242 |
| site_id | BC1 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD E 450 |
| Chain | Residue |
| E | GLY36 |
| E | GLY38 |
| E | PHE39 |
| E | ALA40 |
| E | ASP59 |
| E | ARG60 |
| E | ARG61 |
| E | GLY66 |
| E | ASN67 |
| E | TYR82 |
| E | PRO84 |
| E | HIS85 |
| E | ILE86 |
| E | THR241 |
| E | ASP242 |
| E | TYR243 |
| E | GLY259 |
| E | LEU277 |
| E | GLY363 |
| E | ARG364 |
| E | LEU365 |
| E | TYR371 |
| E | ASN372 |
| E | MET373 |
| E | VAL376 |
| E | HOH405 |
| E | HOH417 |
| E | GDU500 |
| E | HOH625 |
| E | HOH770 |
| site_id | BC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE GDU F 500 |
| Chain | Residue |
| F | HIS109 |
| F | PHE175 |
| F | PHE176 |
| F | TYR179 |
| F | THR180 |
| F | TRP184 |
| F | VAL195 |
| F | THR196 |
| F | ARG198 |
| F | TYR209 |
| F | PHE210 |
| F | THR294 |
| F | ASN296 |
| F | ARG305 |
| F | TYR335 |
| F | TYR370 |
| F | HOH413 |
| F | HOH417 |
| F | HOH418 |
| F | HOH444 |
| F | FAD450 |
| F | HOH711 |
| F | HOH1243 |
| F | HOH1244 |
| site_id | BC3 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD F 450 |
| Chain | Residue |
| F | VAL35 |
| F | GLY36 |
| F | GLY38 |
| F | PHE39 |
| F | ALA40 |
| F | ASP59 |
| F | ARG60 |
| F | ARG61 |
| F | GLY66 |
| F | ASN67 |
| F | TYR82 |
| F | PRO84 |
| F | HIS85 |
| F | ILE86 |
| F | THR241 |
| F | ASP242 |
| F | TYR243 |
| F | THR258 |
| F | GLY259 |
| F | LEU277 |
| F | GLY363 |
| F | ARG364 |
| F | LEU365 |
| F | TYR371 |
| F | ASN372 |
| F | MET373 |
| F | HOH400 |
| F | HOH410 |
| F | HOH430 |
| F | HOH440 |
| F | HOH473 |
| F | GDU500 |
| site_id | BC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE GDU G 500 |
| Chain | Residue |
| G | PRO84 |
| G | HIS109 |
| G | ILE122 |
| G | PHE175 |
| G | PHE176 |
| G | TYR179 |
| G | THR180 |
| G | TRP184 |
| G | VAL195 |
| G | ARG198 |
| G | VAL199 |
| G | TYR209 |
| G | PHE210 |
| G | THR294 |
| G | ASN296 |
| G | ARG305 |
| G | TYR335 |
| G | TYR370 |
| G | FAD450 |
| G | HOH1095 |
| G | HOH1110 |
| G | HOH1245 |
| G | HOH1246 |
| site_id | BC5 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD G 450 |
| Chain | Residue |
| G | VAL35 |
| G | GLY36 |
| G | GLY38 |
| G | PHE39 |
| G | ALA40 |
| G | ASP59 |
| G | ARG60 |
| G | ARG61 |
| G | GLY66 |
| G | ASN67 |
| G | TYR82 |
| G | PRO84 |
| G | HIS85 |
| G | ILE86 |
| G | THR241 |
| G | ASP242 |
| G | TYR243 |
| G | THR258 |
| G | GLY259 |
| G | LEU277 |
| G | TYR334 |
| G | GLY363 |
| G | ARG364 |
| G | TYR371 |
| G | ASN372 |
| G | MET373 |
| G | VAL376 |
| G | HOH405 |
| G | HOH422 |
| G | GDU500 |
| G | HOH611 |
| G | HOH1087 |
| G | HOH1117 |
| site_id | BC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE GDU H 500 |
| Chain | Residue |
| H | PRO84 |
| H | ILE86 |
| H | HIS109 |
| H | PHE175 |
| H | PHE176 |
| H | TYR179 |
| H | THR180 |
| H | TRP184 |
| H | VAL195 |
| H | ARG198 |
| H | TYR209 |
| H | PHE210 |
| H | THR294 |
| H | ASN296 |
| H | ARG305 |
| H | TYR335 |
| H | TYR370 |
| H | HOH432 |
| H | HOH448 |
| H | FAD450 |
| H | HOH451 |
| H | HOH474 |
| H | HOH547 |
| H | HOH587 |
| H | HOH760 |
| H | HOH1247 |
| site_id | BC7 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD H 450 |
| Chain | Residue |
| H | VAL35 |
| H | GLY36 |
| H | GLY38 |
| H | PHE39 |
| H | ALA40 |
| H | ASP59 |
| H | ARG60 |
| H | ARG61 |
| H | GLY66 |
| H | ASN67 |
| H | TYR82 |
| H | PRO84 |
| H | HIS85 |
| H | ILE86 |
| H | THR241 |
| H | ASP242 |
| H | TYR243 |
| H | GLY363 |
| H | ARG364 |
| H | TYR371 |
| H | ASN372 |
| H | MET373 |
| H | HOH411 |
| H | HOH414 |
| H | HOH417 |
| H | HOH420 |
| H | HOH423 |
| H | GDU500 |
| H | HOH848 |
| site_id | BC8 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE GDU I 500 |
| Chain | Residue |
| I | ILE86 |
| I | HIS109 |
| I | ILE122 |
| I | PHE175 |
| I | PHE176 |
| I | TYR179 |
| I | THR180 |
| I | TRP184 |
| I | THR196 |
| I | ARG198 |
| I | TYR209 |
| I | PHE210 |
| I | ASN296 |
| I | ARG305 |
| I | TYR335 |
| I | TYR370 |
| I | HOH410 |
| I | HOH428 |
| I | HOH431 |
| I | FAD450 |
| I | HOH453 |
| I | HOH733 |
| I | HOH1158 |
| I | HOH1160 |
| I | HOH1249 |
| site_id | BC9 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD I 450 |
| Chain | Residue |
| I | VAL35 |
| I | GLY36 |
| I | GLY38 |
| I | PHE39 |
| I | ALA40 |
| I | ASP59 |
| I | ARG60 |
| I | ARG61 |
| I | GLY66 |
| I | ASN67 |
| I | TYR82 |
| I | PRO84 |
| I | HIS85 |
| I | ILE86 |
| I | THR241 |
| I | ASP242 |
| I | TYR243 |
| I | THR258 |
| I | GLY259 |
| I | LEU277 |
| I | GLY363 |
| I | ARG364 |
| I | TYR371 |
| I | ASN372 |
| I | MET373 |
| I | VAL376 |
| I | HOH404 |
| I | HOH407 |
| I | HOH416 |
| I | GDU500 |
| I | HOH1141 |
| I | HOH1167 |
| site_id | CC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE GDU J 500 |
| Chain | Residue |
| J | PRO84 |
| J | ILE86 |
| J | HIS109 |
| J | PHE175 |
| J | PHE176 |
| J | TYR179 |
| J | THR180 |
| J | TRP184 |
| J | VAL195 |
| J | THR196 |
| J | ARG198 |
| J | TYR209 |
| J | PHE210 |
| J | THR294 |
| J | ASN296 |
| J | ARG305 |
| J | TYR335 |
| J | TYR370 |
| J | HOH407 |
| J | HOH425 |
| J | FAD450 |
| J | HOH656 |
| J | HOH1197 |
| J | HOH1209 |
| J | HOH1250 |
| J | HOH1252 |
| site_id | CC2 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD J 450 |
| Chain | Residue |
| J | VAL35 |
| J | GLY36 |
| J | GLY38 |
| J | PHE39 |
| J | ALA40 |
| J | ASP59 |
| J | ARG60 |
| J | ARG61 |
| J | GLY66 |
| J | ASN67 |
| J | TYR82 |
| J | PRO84 |
| J | HIS85 |
| J | ILE86 |
| J | THR241 |
| J | ASP242 |
| J | TYR243 |
| J | ARG244 |
| J | THR258 |
| J | LEU277 |
| J | GLU325 |
| J | GLY363 |
| J | ARG364 |
| J | LEU365 |
| J | TYR371 |
| J | ASN372 |
| J | MET373 |
| J | VAL376 |
| J | HOH421 |
| J | HOH429 |
| J | HOH432 |
| J | HOH433 |
| J | GDU500 |
