3RUA
Specific recognition of N-acetylated substrates and domain flexibility in 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 | 32 |
| Details | BINDING SITE FOR RESIDUE NAD A 343 |
| Chain | Residue |
| A | GLY23 |
| A | THR51 |
| A | GLY52 |
| A | GLY77 |
| A | ASP78 |
| A | ILE79 |
| A | GLN98 |
| A | ALA99 |
| A | ALA100 |
| A | THR117 |
| A | ALA140 |
| A | ALA25 |
| A | ALA141 |
| A | TYR166 |
| A | LYS170 |
| A | TYR193 |
| A | VAL196 |
| A | HOH359 |
| A | HOH362 |
| A | HOH370 |
| A | HOH371 |
| A | HOH374 |
| A | GLY26 |
| A | HOH398 |
| A | HOH402 |
| A | HOH436 |
| A | PHE27 |
| A | ILE28 |
| A | ASP47 |
| A | ASN48 |
| A | PHE49 |
| A | SER50 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 345 |
| Chain | Residue |
| A | ARG4 |
| A | LYS253 |
| A | LYS318 |
| A | HOH435 |
| B | HIS53 |
| B | GLN54 |
| B | TYR55 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 346 |
| Chain | Residue |
| A | HIS53 |
| A | GLN54 |
| A | TYR55 |
| B | ARG4 |
| B | LYS253 |
| B | LYS318 |
| 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 | PHE49 |
| 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 | VAL196 |
| B | HOH346 |
| B | HOH352 |
| B | HOH359 |
| B | HOH362 |
| B | HOH378 |
| B | HOH381 |
| B | HOH383 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD C 343 |
| Chain | Residue |
| C | ASN195 |
| C | VAL196 |
| C | GLN201 |
| C | HOH363 |
| C | HOH365 |
| C | HOH368 |
| C | HOH371 |
| C | HOH388 |
| C | HOH401 |
| C | GLY23 |
| C | ALA25 |
| C | GLY26 |
| C | PHE27 |
| C | ILE28 |
| C | ASP47 |
| C | ASN48 |
| C | PHE49 |
| 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 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD D 343 |
| Chain | Residue |
| D | GLY23 |
| D | ALA25 |
| D | GLY26 |
| D | PHE27 |
| D | ILE28 |
| D | ASP47 |
| D | ASN48 |
| D | PHE49 |
| D | SER50 |
| D | THR51 |
| D | GLY52 |
| D | GLY77 |
| D | ASP78 |
| D | ILE79 |
| D | GLN98 |
| D | ALA99 |
| D | ALA100 |
| D | THR117 |
| D | ALA140 |
| D | ALA141 |
| D | TYR166 |
| D | LYS170 |
| D | TYR193 |
| D | ASN195 |
| D | VAL196 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21384454, ECO:0000269|PubMed:21810411, ECO:0000312|PDB:3LU1, ECO:0000312|PDB:3RU7, ECO:0000312|PDB:3RU9, ECO:0000312|PDB:3RUA, ECO:0000312|PDB:3RUC, ECO:0000312|PDB:3RUD, ECO:0000312|PDB:3RUE, ECO:0000312|PDB:3RUF, ECO:0000312|PDB:3RUH |
| Chain | Residue | Details |
| A | GLY23 | |
| B | ASP78 | |
| B | GLN98 | |
| B | TYR166 | |
| B | LYS170 | |
| B | VAL196 | |
| C | GLY23 | |
| C | ASP47 | |
| C | ASP78 | |
| C | GLN98 | |
| C | TYR166 | |
| A | ASP47 | |
| C | LYS170 | |
| C | VAL196 | |
| D | GLY23 | |
| D | ASP47 | |
| D | ASP78 | |
| D | GLN98 | |
| D | TYR166 | |
| D | LYS170 | |
| D | VAL196 | |
| A | ASP78 | |
| A | GLN98 | |
| A | TYR166 | |
| A | LYS170 | |
| A | VAL196 | |
| B | GLY23 | |
| B | ASP47 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21384454, ECO:0000269|PubMed:21810411, ECO:0000312|PDB:3RUA, ECO:0000312|PDB:3RUC |
| Chain | Residue | Details |
| A | THR117 | |
| B | THR117 | |
| C | THR117 | |
| D | THR117 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21384454, ECO:0000269|PubMed:21810411 |
| Chain | Residue | Details |
| A | SER142 | |
| B | TYR225 | |
| B | ARG234 | |
| B | ARG299 | |
| C | SER142 | |
| C | TYR193 | |
| C | VAL210 | |
| C | TYR225 | |
| C | ARG234 | |
| C | ARG299 | |
| D | SER142 | |
| A | TYR193 | |
| D | TYR193 | |
| D | VAL210 | |
| D | TYR225 | |
| D | ARG234 | |
| D | ARG299 | |
| A | VAL210 | |
| A | TYR225 | |
| A | ARG234 | |
| A | ARG299 | |
| B | SER142 | |
| B | TYR193 | |
| B | VAL210 |
