6JP9
Crsytal structure of a XMP complexed ATPPase subunit of M. jannaschii GMP synthetase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003921 | molecular_function | GMP synthase activity |
| A | 0003922 | molecular_function | GMP synthase (glutamine-hydrolyzing) activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006177 | biological_process | GMP biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| B | 0003921 | molecular_function | GMP synthase activity |
| B | 0003922 | molecular_function | GMP synthase (glutamine-hydrolyzing) activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006177 | biological_process | GMP biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| C | 0003921 | molecular_function | GMP synthase activity |
| C | 0003922 | molecular_function | GMP synthase (glutamine-hydrolyzing) activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0006164 | biological_process | purine nucleotide biosynthetic process |
| C | 0006177 | biological_process | GMP biosynthetic process |
| C | 0016874 | molecular_function | ligase activity |
| D | 0003921 | molecular_function | GMP synthase activity |
| D | 0003922 | molecular_function | GMP synthase (glutamine-hydrolyzing) activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0006164 | biological_process | purine nucleotide biosynthetic process |
| D | 0006177 | biological_process | GMP biosynthetic process |
| D | 0016874 | molecular_function | ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue XMP A 401 |
| Chain | Residue |
| A | ARG102 |
| A | HOH522 |
| B | ARG249 |
| A | PRO189 |
| A | GLY190 |
| A | PRO191 |
| A | GLN231 |
| A | LYS302 |
| A | THR306 |
| A | ILE307 |
| A | GLU308 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for residue XMP B 401 |
| Chain | Residue |
| A | ARG249 |
| B | ARG102 |
| B | PRO189 |
| B | GLY190 |
| B | PRO191 |
| B | TRP230 |
| B | GLN231 |
| B | ALA265 |
| B | LYS302 |
| B | THR306 |
| B | ILE307 |
| B | GLU308 |
| B | HOH513 |
| B | HOH569 |
| B | HOH574 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue XMP C 401 |
| Chain | Residue |
| C | ARG102 |
| C | PRO189 |
| C | GLY190 |
| C | PRO191 |
| C | TRP230 |
| C | GLN231 |
| C | LYS302 |
| C | THR306 |
| C | ILE307 |
| C | GLU308 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue XMP D 401 |
| Chain | Residue |
| C | ARG249 |
| D | ARG102 |
| D | PRO189 |
| D | GLY190 |
| D | PRO191 |
| D | TRP230 |
| D | GLN231 |
| D | LYS302 |
| D | THR306 |
| D | ILE307 |
| D | GLU308 |
| D | HOH511 |
| D | HOH529 |
| D | HOH553 |
| D | HOH557 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue PGE D 402 |
| Chain | Residue |
| A | ASP133 |
| A | TYR165 |
| D | ALA148 |
| D | LEU149 |
| D | PRO150 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MLA D 403 |
| Chain | Residue |
| D | SER29 |
| D | GLY31 |
| D | VAL32 |
| D | ASP33 |
| D | SER34 |
| D | HOH502 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | SER29 | |
| B | SER29 | |
| C | SER29 | |
| D | SER29 |
