6C6B
Co-crystal structure of adenylyl-sulfate kinase from Cryptococcus neoformans bound to ADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000103 | biological_process | sulfate assimilation |
| A | 0004020 | molecular_function | adenylylsulfate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
| B | 0000103 | biological_process | sulfate assimilation |
| B | 0004020 | molecular_function | adenylylsulfate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| B | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
| C | 0000103 | biological_process | sulfate assimilation |
| C | 0004020 | molecular_function | adenylylsulfate kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016310 | biological_process | phosphorylation |
| C | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
| D | 0000103 | biological_process | sulfate assimilation |
| D | 0004020 | molecular_function | adenylylsulfate kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016310 | biological_process | phosphorylation |
| D | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
| E | 0000103 | biological_process | sulfate assimilation |
| E | 0004020 | molecular_function | adenylylsulfate kinase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0016301 | molecular_function | kinase activity |
| E | 0016310 | biological_process | phosphorylation |
| E | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
| F | 0000103 | biological_process | sulfate assimilation |
| F | 0004020 | molecular_function | adenylylsulfate kinase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0016301 | molecular_function | kinase activity |
| F | 0016310 | biological_process | phosphorylation |
| F | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue ADP A 300 |
| Chain | Residue |
| A | LEU33 |
| A | VAL182 |
| A | ASP183 |
| A | VAL184 |
| A | HOH410 |
| A | HOH423 |
| A | HOH428 |
| D | ALA203 |
| A | ALA35 |
| A | SER36 |
| A | GLY37 |
| A | LYS38 |
| A | SER39 |
| A | THR40 |
| A | ARG143 |
| A | THR179 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 301 |
| Chain | Residue |
| A | GLU120 |
| A | PHE128 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue ADP B 300 |
| Chain | Residue |
| B | LEU33 |
| B | ALA35 |
| B | SER36 |
| B | GLY37 |
| B | LYS38 |
| B | SER39 |
| B | THR40 |
| B | ARG143 |
| B | THR179 |
| B | VAL182 |
| B | ASP183 |
| B | VAL184 |
| B | HOH423 |
| B | HOH440 |
| B | HOH467 |
| B | HOH472 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 301 |
| Chain | Residue |
| B | GLU120 |
| B | PHE128 |
| B | GLU174 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| B | VAL80 |
| B | GLU81 |
| B | ARG84 |
| B | HOH465 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | binding site for residue ADP C 300 |
| Chain | Residue |
| A | ALA203 |
| C | LEU33 |
| C | ALA35 |
| C | SER36 |
| C | GLY37 |
| C | LYS38 |
| C | SER39 |
| C | THR40 |
| C | ILE41 |
| C | ARG143 |
| C | THR179 |
| C | VAL182 |
| C | ASP183 |
| C | HOH416 |
| C | HOH426 |
| C | HOH427 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | binding site for residue ADP D 300 |
| Chain | Residue |
| D | LEU33 |
| D | ALA35 |
| D | SER36 |
| D | GLY37 |
| D | LYS38 |
| D | SER39 |
| D | THR40 |
| D | ARG143 |
| D | THR179 |
| D | VAL182 |
| D | ASP183 |
| D | VAL184 |
| D | HOH403 |
| D | HOH422 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue ADP E 300 |
| Chain | Residue |
| E | LEU33 |
| E | ALA35 |
| E | SER36 |
| E | GLY37 |
| E | LYS38 |
| E | SER39 |
| E | THR40 |
| E | THR179 |
| E | VAL182 |
| E | VAL184 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | binding site for residue ADP F 300 |
| Chain | Residue |
| F | LEU33 |
| F | ALA35 |
| F | SER36 |
| F | GLY37 |
| F | LYS38 |
| F | SER39 |
| F | THR40 |
| F | ARG143 |
| F | THR179 |
| F | VAL182 |
| F | ASP183 |
| F | VAL184 |
| F | HOH403 |
| F | HOH407 |
| F | HOH408 |
