3LU1
Crystal Structure Analysis of WbgU: a UDP-GalNAc 4-epimerase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003974 | molecular_function | UDP-N-acetylglucosamine 4-epimerase activity |
| A | 0009243 | biological_process | O antigen biosynthetic process |
| A | 0016853 | molecular_function | isomerase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003974 | molecular_function | UDP-N-acetylglucosamine 4-epimerase activity |
| B | 0009243 | biological_process | O antigen biosynthetic process |
| B | 0016853 | molecular_function | isomerase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003974 | molecular_function | UDP-N-acetylglucosamine 4-epimerase activity |
| C | 0009243 | biological_process | O antigen biosynthetic process |
| C | 0016853 | molecular_function | isomerase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003974 | molecular_function | UDP-N-acetylglucosamine 4-epimerase activity |
| D | 0009243 | biological_process | O antigen biosynthetic process |
| D | 0016853 | molecular_function | isomerase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD A 343 |
| Chain | Residue |
| A | GLY23 |
| A | GLY52 |
| A | GLY77 |
| A | ASP78 |
| A | ILE79 |
| A | GLN98 |
| A | ALA99 |
| A | ALA100 |
| A | THR117 |
| A | ALA140 |
| A | ALA141 |
| A | ALA25 |
| A | TYR166 |
| A | LYS170 |
| A | TYR193 |
| A | ASN195 |
| A | VAL196 |
| A | UD2344 |
| A | HOH355 |
| A | HOH364 |
| A | HOH374 |
| A | HOH376 |
| A | GLY26 |
| A | HOH391 |
| A | PHE27 |
| A | ILE28 |
| A | ASP47 |
| A | ASN48 |
| A | SER50 |
| A | THR51 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE UD2 A 344 |
| Chain | Residue |
| A | SER103 |
| A | SER142 |
| A | SER143 |
| A | SER144 |
| A | TYR166 |
| A | TYR193 |
| A | ASN195 |
| A | VAL210 |
| A | LYS213 |
| A | TRP214 |
| A | TYR225 |
| A | ILE226 |
| A | ASN227 |
| A | ARG234 |
| A | LEU271 |
| A | ARG299 |
| A | ASP302 |
| A | VAL303 |
| A | NAD343 |
| A | HOH350 |
| A | HOH377 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GLY A 345 |
| Chain | Residue |
| A | VAL134 |
| A | GLN135 |
| A | GLY185 |
| A | LYS187 |
| A | LYS257 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD B 343 |
| Chain | Residue |
| B | GLY23 |
| B | ALA25 |
| B | GLY26 |
| B | PHE27 |
| B | ILE28 |
| B | ASP47 |
| B | ASN48 |
| B | SER50 |
| B | THR51 |
| B | GLY52 |
| B | GLY77 |
| B | ASP78 |
| B | ILE79 |
| B | GLN98 |
| B | ALA99 |
| B | ALA100 |
| B | THR117 |
| B | ALA140 |
| B | ALA141 |
| B | TYR166 |
| B | LYS170 |
| B | TYR193 |
| B | ASN195 |
| B | VAL196 |
| B | UD2344 |
| B | HOH354 |
| B | HOH362 |
| B | HOH367 |
| B | HOH378 |
| B | HOH383 |
| B | HOH399 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE UD2 B 344 |
| Chain | Residue |
| B | ASN227 |
| B | THR232 |
| B | ARG234 |
| B | LEU271 |
| B | ARG299 |
| B | ASP302 |
| B | VAL303 |
| B | NAD343 |
| B | HOH361 |
| B | HOH380 |
| B | HOH401 |
| B | HOH402 |
| B | SER103 |
| B | SER142 |
| B | SER143 |
| B | SER144 |
| B | TYR166 |
| B | TYR193 |
| B | ASN195 |
| B | ALA209 |
| B | VAL210 |
| B | LYS213 |
| B | TYR225 |
| B | ILE226 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GLY B 345 |
| Chain | Residue |
| B | LYS253 |
| B | ASP254 |
| B | SER255 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD C 343 |
| Chain | Residue |
| C | GLY23 |
| C | ALA25 |
| C | GLY26 |
| C | PHE27 |
| C | ILE28 |
| C | ASP47 |
| C | ASN48 |
| C | SER50 |
| C | THR51 |
| C | GLY52 |
| C | GLY77 |
| C | ASP78 |
| C | ILE79 |
| C | GLN98 |
| C | ALA99 |
| C | ALA100 |
| C | THR117 |
| C | ALA140 |
| C | ALA141 |
| C | TYR166 |
| C | LYS170 |
| C | TYR193 |
| C | ASN195 |
| C | VAL196 |
| C | UD2344 |
| C | HOH361 |
| C | HOH376 |
| C | HOH386 |
| site_id | AC8 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE UD2 C 344 |
| Chain | Residue |
| C | SER103 |
| C | SER142 |
| C | SER143 |
| C | SER144 |
| C | TYR166 |
| C | TYR193 |
| C | ASN195 |
| C | ALA209 |
| C | VAL210 |
| C | LYS213 |
| C | TYR225 |
| C | ILE226 |
| C | ASN227 |
| C | THR232 |
| C | ARG234 |
| C | LEU271 |
| C | ARG299 |
| C | ASP302 |
| C | VAL303 |
| C | NAD343 |
| C | GLY346 |
| C | HOH358 |
| C | HOH360 |
| C | HOH379 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 345 |
| Chain | Residue |
| B | ARG304 |
| B | HIS305 |
| C | ARG304 |
| C | HIS305 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GLY C 346 |
| Chain | Residue |
| C | ASN227 |
| C | ARG296 |
| C | ARG299 |
| C | UD2344 |
| site_id | BC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD D 344 |
| Chain | Residue |
| D | GLY23 |
| D | ALA25 |
| D | GLY26 |
| D | PHE27 |
| D | ILE28 |
| D | ASP47 |
| D | ASN48 |
| D | SER50 |
| D | THR51 |
| D | GLY52 |
| D | GLY77 |
| D | ASP78 |
| D | ILE79 |
| D | GLN98 |
| D | ALA99 |
| D | ALA100 |
| D | ALA140 |
| D | ALA141 |
| D | TYR166 |
| D | LYS170 |
| D | TYR193 |
| D | ASN195 |
| D | VAL196 |
| D | UD2343 |
| D | HOH349 |
| D | HOH379 |
| site_id | BC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE UD2 D 343 |
| Chain | Residue |
| D | SER103 |
| D | SER142 |
| D | SER143 |
| D | SER144 |
| D | TYR166 |
| D | TYR193 |
| D | ASN195 |
| D | ALA209 |
| D | VAL210 |
| D | LYS213 |
| D | TRP214 |
| D | TYR225 |
| D | ILE226 |
| D | ASN227 |
| D | ARG234 |
| D | LEU271 |
| D | ARG299 |
| D | ASP302 |
| D | VAL303 |
| D | SER306 |
| D | NAD344 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA D 345 |
| Chain | Residue |
| D | HOH380 |
| D | HOH381 |
| D | HOH382 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 346 |
| Chain | Residue |
| A | HIS53 |
| A | GLN54 |
| A | TYR55 |
| D | ARG4 |
| D | LYS253 |
| D | LYS318 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 347 |
| Chain | Residue |
| A | ARG4 |
| A | LYS253 |
| A | LYS318 |
| D | HIS53 |
| D | GLN54 |
| D | TYR55 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GLY D 348 |
| Chain | Residue |
| A | ARG304 |
| A | HIS305 |
| D | ARG304 |
| D | HIS305 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 64 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21384454","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21810411","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3LU1","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3RU7","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3RU9","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3RUA","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3RUC","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3RUD","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3RUE","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3RUF","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3RUH","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21384454","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21810411","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3RUA","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3RUC","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 48 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21384454","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21810411","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
