4J2O
Crystal structure of NADP-bound WbjB from A. baumannii community strain D1279779
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| A | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| B | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| B | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| C | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| C | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| D | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| D | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| E | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| E | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| F | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| F | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAP A 400 |
| Chain | Residue |
| A | GLY11 |
| A | ASP60 |
| A | VAL61 |
| A | ALA80 |
| A | ALA81 |
| A | ALA82 |
| A | LYS84 |
| A | THR99 |
| A | LEU122 |
| A | THR124 |
| A | LYS138 |
| A | THR13 |
| A | TYR164 |
| A | GLY165 |
| A | HOH502 |
| D | ASP38 |
| D | LYS40 |
| A | GLY14 |
| A | SER15 |
| A | PHE16 |
| A | SER36 |
| A | ARG37 |
| A | ASP38 |
| A | LYS41 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAP B 400 |
| Chain | Residue |
| B | GLY11 |
| B | THR13 |
| B | GLY14 |
| B | SER15 |
| B | PHE16 |
| B | SER36 |
| B | ARG37 |
| B | ASP38 |
| B | LYS41 |
| B | ASP60 |
| B | VAL61 |
| B | ALA80 |
| B | ALA81 |
| B | ALA82 |
| B | LYS84 |
| B | THR99 |
| B | LEU122 |
| B | THR124 |
| B | LYS138 |
| B | TYR164 |
| B | GLY165 |
| B | ASN166 |
| B | VAL167 |
| B | HOH502 |
| F | LYS40 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAP C 400 |
| Chain | Residue |
| C | GLY11 |
| C | THR13 |
| C | GLY14 |
| C | SER15 |
| C | PHE16 |
| C | SER36 |
| C | ARG37 |
| C | ASP38 |
| C | LYS41 |
| C | ASP60 |
| C | VAL61 |
| C | ALA80 |
| C | ALA81 |
| C | ALA82 |
| C | LYS84 |
| C | THR99 |
| C | LEU122 |
| C | THR124 |
| C | LYS138 |
| C | TYR164 |
| E | LYS40 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAP D 400 |
| Chain | Residue |
| A | LYS40 |
| D | GLY11 |
| D | THR13 |
| D | GLY14 |
| D | SER15 |
| D | PHE16 |
| D | SER36 |
| D | ARG37 |
| D | ASP38 |
| D | LYS41 |
| D | GLY59 |
| D | ASP60 |
| D | VAL61 |
| D | ALA80 |
| D | ALA81 |
| D | ALA82 |
| D | LYS84 |
| D | LEU122 |
| D | SER123 |
| D | THR124 |
| D | LYS138 |
| D | TYR164 |
| D | GLY165 |
| D | ASN166 |
| D | HOH509 |
| D | HOH521 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAP E 400 |
| Chain | Residue |
| E | GLY14 |
| E | SER15 |
| E | PHE16 |
| E | SER36 |
| E | ARG37 |
| E | ASP38 |
| E | LYS41 |
| E | ASP60 |
| E | VAL61 |
| E | ALA80 |
| E | ALA81 |
| E | ALA82 |
| E | LYS84 |
| E | THR99 |
| E | THR124 |
| E | LYS138 |
| E | TYR164 |
| E | GLY165 |
| E | ASN166 |
| C | LYS40 |
| E | GLY11 |
| E | THR13 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAP F 400 |
| Chain | Residue |
| B | LYS40 |
| F | GLY11 |
| F | THR13 |
| F | GLY14 |
| F | SER15 |
| F | PHE16 |
| F | SER36 |
| F | ARG37 |
| F | ASP38 |
| F | LYS41 |
| F | ASP60 |
| F | VAL61 |
| F | ALA80 |
| F | ALA81 |
| F | ALA82 |
| F | LYS84 |
| F | THR99 |
| F | SER123 |
| F | THR124 |
| F | LYS138 |
| F | TYR164 |
| F | GLY165 |
| F | ASN166 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (GalNAc...) threonine","evidences":[{"source":"PubMed","id":"10076062","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






