3RUC
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 | 31 |
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 | SER142 |
A | TYR166 |
A | LYS170 |
A | TYR193 |
A | ASN195 |
A | VAL196 |
A | UD2344 |
A | HOH346 |
A | HOH355 |
A | HOH359 |
A | GLY26 |
A | HOH372 |
A | HOH402 |
A | PHE27 |
A | ILE28 |
A | ASP47 |
A | ASN48 |
A | SER50 |
A | THR51 |
site_id | AC2 |
Number of Residues | 23 |
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 | ALA209 |
A | VAL210 |
A | LYS213 |
A | TYR225 |
A | ILE226 |
A | ASN227 |
A | THR232 |
A | ARG234 |
A | LEU271 |
A | ARG299 |
A | ASP302 |
A | NAD343 |
A | HOH360 |
A | HOH413 |
A | HOH426 |
A | HOH433 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 345 |
Chain | Residue |
A | ARG4 |
A | LYS253 |
A | LYS318 |
B | HIS53 |
B | GLN54 |
B | TYR55 |
site_id | AC4 |
Number of Residues | 29 |
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 | HOH356 |
B | HOH359 |
B | HOH368 |
B | HOH373 |
site_id | AC5 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE UD2 B 344 |
Chain | Residue |
B | TRP214 |
B | TYR225 |
B | ILE226 |
B | ASN227 |
B | THR232 |
B | ARG234 |
B | LEU271 |
B | ARG299 |
B | ASP302 |
B | VAL303 |
B | SER306 |
B | NAD343 |
B | HOH352 |
B | HOH404 |
B | SER103 |
B | SER142 |
B | SER143 |
B | SER144 |
B | TYR166 |
B | TYR193 |
B | ASN195 |
B | ALA209 |
B | VAL210 |
B | LYS213 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 345 |
Chain | Residue |
A | HIS53 |
A | GLN54 |
A | TYR55 |
B | ARG4 |
B | LYS253 |
B | LYS318 |
site_id | AC7 |
Number of Residues | 33 |
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 | ARG80 |
C | GLN98 |
C | ALA99 |
C | ALA100 |
C | THR117 |
C | ALA140 |
C | ALA141 |
C | TYR166 |
C | LYS170 |
C | TYR193 |
C | ASN195 |
C | VAL196 |
C | GLN201 |
C | UD2344 |
C | HOH370 |
C | HOH372 |
C | HOH376 |
C | HOH385 |
C | HOH403 |
C | HOH406 |
site_id | AC8 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE UD2 C 344 |
Chain | Residue |
C | GLY102 |
C | SER103 |
C | SER142 |
C | SER143 |
C | SER144 |
C | TYR166 |
C | TYR193 |
C | ASN195 |
C | ALA209 |
C | VAL210 |
C | LYS213 |
C | TRP214 |
C | TYR225 |
C | ILE226 |
C | ASN227 |
C | THR232 |
C | ARG234 |
C | LEU271 |
C | ARG299 |
C | ASP302 |
C | VAL303 |
C | NAD343 |
C | HOH377 |
C | HOH432 |
site_id | AC9 |
Number of Residues | 31 |
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 | 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 |
D | GLN201 |
D | UD2344 |
D | HOH355 |
D | HOH360 |
D | HOH371 |
D | HOH374 |
D | HOH379 |
site_id | BC1 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE UD2 D 344 |
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 | THR232 |
D | ARG234 |
D | LEU271 |
D | ARG299 |
D | ASP302 |
D | VAL303 |
D | SER306 |
D | NAD343 |
D | HOH390 |
D | HOH397 |
D | HOH409 |
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 |