3DR7
GDP-perosamine synthase from Caulobacter crescentus with bound GDP-3-deoxyperosamine
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 | 0016740 | molecular_function | transferase activity |
| 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 | 0016740 | molecular_function | transferase activity |
| 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 | 0016740 | molecular_function | transferase activity |
| 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 | 0016740 | molecular_function | transferase activity |
| 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 | 21 |
| Details | BINDING SITE FOR RESIDUE GPD A 500 |
| Chain | Residue |
| A | ALA10 |
| A | ARG315 |
| A | HOH589 |
| A | HOH670 |
| A | HOH763 |
| B | THR29 |
| B | TRP30 |
| B | ILE31 |
| B | SER32 |
| B | ARG220 |
| B | TYR221 |
| A | PRO12 |
| B | ARG231 |
| B | HOH1145 |
| A | TYR86 |
| A | PHE183 |
| A | GLY184 |
| A | ASN185 |
| A | LLP186 |
| A | TRP286 |
| A | GLU313 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE GPD A 501 |
| Chain | Residue |
| A | THR29 |
| A | TRP30 |
| A | ILE31 |
| A | SER32 |
| A | VAL34 |
| A | ARG220 |
| A | TYR221 |
| A | HOH643 |
| A | HOH671 |
| A | HOH694 |
| A | HOH705 |
| A | HOH709 |
| B | ALA10 |
| B | PRO12 |
| B | TYR86 |
| B | PHE183 |
| B | GLY184 |
| B | ASN185 |
| B | LLP186 |
| B | TRP286 |
| B | GLU313 |
| B | ARG315 |
| B | HOH1153 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 1040 |
| Chain | Residue |
| B | THR332 |
| B | ASP333 |
| C | ILE121 |
| C | THR122 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE GPD D 500 |
| Chain | Residue |
| C | ALA10 |
| C | PRO12 |
| C | TYR86 |
| C | PHE183 |
| C | GLY184 |
| C | ASN185 |
| C | LLP186 |
| C | TRP286 |
| C | GLU313 |
| C | ARG315 |
| C | HOH469 |
| D | THR29 |
| D | TRP30 |
| D | ILE31 |
| D | SER32 |
| D | ARG220 |
| D | TYR221 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE GPD D 501 |
| Chain | Residue |
| C | THR29 |
| C | TRP30 |
| C | ILE31 |
| C | SER32 |
| C | ARG220 |
| D | SER8 |
| D | ALA10 |
| D | PRO12 |
| D | TYR86 |
| D | PHE183 |
| D | GLY184 |
| D | ASN185 |
| D | LLP186 |
| D | TRP286 |
| D | GLU313 |
| D | ARG315 |
| D | PHE318 |
| D | HOH1200 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D 1041 |
| Chain | Residue |
| D | ARG108 |
| D | THR273 |
| D | LYS274 |
| D | HIS276 |
| D | HOH1126 |
| D | HOH1160 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"UniProtKB","id":"Q8ZNF3","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"18795799","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b9h |
| Chain | Residue | Details |
| A | TYR86 | |
| A | ASP157 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b9h |
| Chain | Residue | Details |
| B | TYR86 | |
| B | ASP157 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b9h |
| Chain | Residue | Details |
| C | TYR86 | |
| C | ASP157 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b9h |
| Chain | Residue | Details |
| D | TYR86 | |
| D | ASP157 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b9h |
| Chain | Residue | Details |
| A | SER32 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b9h |
| Chain | Residue | Details |
| B | SER32 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b9h |
| Chain | Residue | Details |
| C | SER32 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b9h |
| Chain | Residue | Details |
| D | SER32 |
