3DR4
GDP-perosamine synthase K186A mutant from Caulobacter crescentus with bound sugar ligand
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000271 | biological_process | polysaccharide biosynthetic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| A | 0009243 | biological_process | O antigen biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0102933 | molecular_function | GDP-4-dehydro-6-deoxy-D-mannose-4-aminotransferase activity |
| B | 0000271 | biological_process | polysaccharide biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| B | 0009243 | biological_process | O antigen biosynthetic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0102933 | molecular_function | GDP-4-dehydro-6-deoxy-D-mannose-4-aminotransferase activity |
| C | 0000271 | biological_process | polysaccharide biosynthetic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| C | 0009243 | biological_process | O antigen biosynthetic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0102933 | molecular_function | GDP-4-dehydro-6-deoxy-D-mannose-4-aminotransferase activity |
| D | 0000271 | biological_process | polysaccharide biosynthetic process |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| D | 0009243 | biological_process | O antigen biosynthetic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0102933 | molecular_function | GDP-4-dehydro-6-deoxy-D-mannose-4-aminotransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE G4M A 500 |
| Chain | Residue |
| A | SER8 |
| A | GLU160 |
| A | SER181 |
| A | PHE183 |
| A | GLY184 |
| A | ASN185 |
| A | GLU313 |
| A | ARG315 |
| B | THR29 |
| B | TRP30 |
| B | ILE31 |
| A | ALA10 |
| B | SER32 |
| B | ARG220 |
| B | TYR221 |
| B | ASN229 |
| A | PRO12 |
| A | ASN59 |
| A | GLY60 |
| A | THR61 |
| A | TYR86 |
| A | ASP157 |
| A | ALA159 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE G4M B 500 |
| Chain | Residue |
| A | THR29 |
| A | TRP30 |
| A | ILE31 |
| A | SER32 |
| A | ARG220 |
| A | TYR221 |
| A | ASN229 |
| B | ALA10 |
| B | PRO12 |
| B | ASN59 |
| B | GLY60 |
| B | THR61 |
| B | TYR86 |
| B | ASP157 |
| B | ALA159 |
| B | GLU160 |
| B | SER181 |
| B | PHE183 |
| B | GLY184 |
| B | ASN185 |
| B | GLU313 |
| B | ARG315 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE G4M C 500 |
| Chain | Residue |
| C | ALA10 |
| C | PRO12 |
| C | ASN59 |
| C | GLY60 |
| C | THR61 |
| C | TYR86 |
| C | ASP157 |
| C | ALA159 |
| C | GLU160 |
| C | SER181 |
| C | PHE183 |
| C | GLY184 |
| C | ASN185 |
| C | GLU313 |
| C | ARG315 |
| D | THR29 |
| D | TRP30 |
| D | ILE31 |
| D | SER32 |
| D | ARG220 |
| D | TYR221 |
| D | ASN229 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE G4M D 500 |
| Chain | Residue |
| C | THR29 |
| C | TRP30 |
| C | ILE31 |
| C | SER32 |
| C | ARG220 |
| C | TYR221 |
| C | ASN229 |
| D | ALA10 |
| D | PRO12 |
| D | ASN59 |
| D | GLY60 |
| D | THR61 |
| D | TYR86 |
| D | ASP157 |
| D | ALA159 |
| D | GLU160 |
| D | SER181 |
| D | PHE183 |
| D | GLY184 |
| D | ASN185 |
| D | GLU313 |
| D | ARG315 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 1260 |
| Chain | Residue |
| B | LEU292 |
| B | GLY293 |
| B | ASP344 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 1261 |
| Chain | Residue |
| B | LEU296 |
| B | THR298 |
| B | THR299 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:Q8ZNF3, ECO:0000303|PubMed:18795799 |
| Chain | Residue | Details |
| A | ARG211 | |
| B | ARG211 | |
| C | ARG211 | |
| D | ARG211 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cl1 |
| Chain | Residue | Details |
| A | TYR86 | |
| A | ASP157 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cl1 |
| Chain | Residue | Details |
| B | TYR86 | |
| B | ASP157 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cl1 |
| Chain | Residue | Details |
| C | TYR86 | |
| C | ASP157 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cl1 |
| Chain | Residue | Details |
| D | TYR86 | |
| D | ASP157 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cl1 |
| Chain | Residue | Details |
| A | SER32 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cl1 |
| Chain | Residue | Details |
| B | SER32 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cl1 |
| Chain | Residue | Details |
| C | SER32 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cl1 |
| Chain | Residue | Details |
| D | SER32 |
