5URS
Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with IMP and the inhibitor P178
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003938 | molecular_function | IMP dehydrogenase activity |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003938 | molecular_function | IMP dehydrogenase activity |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0003938 | molecular_function | IMP dehydrogenase activity |
| C | 0006164 | biological_process | purine nucleotide biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0003938 | molecular_function | IMP dehydrogenase activity |
| D | 0006164 | biological_process | purine nucleotide biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0003938 | molecular_function | IMP dehydrogenase activity |
| E | 0006164 | biological_process | purine nucleotide biosynthetic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0003938 | molecular_function | IMP dehydrogenase activity |
| F | 0006164 | biological_process | purine nucleotide biosynthetic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0003938 | molecular_function | IMP dehydrogenase activity |
| G | 0006164 | biological_process | purine nucleotide biosynthetic process |
| G | 0016491 | molecular_function | oxidoreductase activity |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0003938 | molecular_function | IMP dehydrogenase activity |
| H | 0006164 | biological_process | purine nucleotide biosynthetic process |
| H | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue IMP A 501 |
| Chain | Residue |
| A | ALA49 |
| A | GLY343 |
| A | MET362 |
| A | LEU363 |
| A | GLY364 |
| A | SER365 |
| A | TYR388 |
| A | GLY390 |
| A | MET391 |
| A | GLY392 |
| A | GLU416 |
| A | MET51 |
| A | 8LA502 |
| A | HOH617 |
| A | HOH628 |
| A | ASN280 |
| A | GLY305 |
| A | SER306 |
| A | ILE307 |
| A | CYS308 |
| A | ASP341 |
| A | GLY342 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue 8LA A 502 |
| Chain | Residue |
| A | THR252 |
| A | ALA253 |
| A | HIS254 |
| A | SER257 |
| A | GLY259 |
| A | THR310 |
| A | GLY392 |
| A | GLU416 |
| A | IMP501 |
| C | ALA441 |
| C | GLY444 |
| C | TYR445 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue K A 503 |
| Chain | Residue |
| A | GLU470 |
| A | SER471 |
| A | HIS472 |
| B | GLY303 |
| B | GLY305 |
| B | CYS308 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | LEU11 |
| A | ARG462 |
| A | MET463 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue K A 505 |
| Chain | Residue |
| A | GLY303 |
| A | GLY305 |
| A | CYS308 |
| C | GLU470 |
| C | SER471 |
| C | HIS472 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | binding site for residue IMP B 500 |
| Chain | Residue |
| B | ALA49 |
| B | GLY305 |
| B | SER306 |
| B | CYS308 |
| B | ASP341 |
| B | GLY342 |
| B | GLY343 |
| B | GLY364 |
| B | SER365 |
| B | TYR388 |
| B | GLY390 |
| B | MET391 |
| B | GLY392 |
| B | GLU416 |
| B | GLY417 |
| B | 8LA501 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | binding site for residue 8LA B 501 |
| Chain | Residue |
| A | GLY444 |
| B | ALA253 |
| B | HIS254 |
| B | SER257 |
| B | GLY259 |
| B | VAL260 |
| B | MET391 |
| B | GLY392 |
| B | GLU416 |
| B | IMP500 |
| B | HOH621 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue K B 502 |
| Chain | Residue |
| B | GLU470 |
| B | SER471 |
| B | HIS472 |
| D | GLY303 |
| D | PRO304 |
| D | GLY305 |
| D | CYS308 |
| site_id | AC9 |
| Number of Residues | 23 |
| Details | binding site for residue IMP C 501 |
| Chain | Residue |
| C | MET391 |
| C | GLY392 |
| C | GLU416 |
| C | GLY417 |
| C | 8LA502 |
| C | HOH613 |
| C | HOH620 |
| C | ALA49 |
| C | MET51 |
| C | ASN280 |
| C | GLY305 |
| C | SER306 |
| C | ILE307 |
| C | CYS308 |
| C | ASP341 |
| C | GLY342 |
| C | GLY343 |
| C | MET362 |
| C | LEU363 |
| C | GLY364 |
| C | SER365 |
| C | TYR388 |
| C | GLY390 |
| site_id | AD1 |
| Number of Residues | 15 |
| Details | binding site for residue 8LA C 502 |
| Chain | Residue |
| C | THR252 |
| C | ALA253 |
| C | HIS254 |
| C | SER257 |
| C | GLY259 |
| C | VAL260 |
| C | MET391 |
| C | GLY392 |
| C | VAL414 |
| C | GLU416 |
| C | IMP501 |
| D | LEU26 |
| D | ALA441 |
| D | GLY444 |
| D | TYR445 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 C 503 |
| Chain | Residue |
| C | ARG332 |
| C | GLY357 |
| C | ARG455 |
| C | GLU456 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 C 504 |
| Chain | Residue |
| C | ARG311 |
| C | VAL312 |
| C | HOH604 |
| D | ASP14 |
| D | LEU17 |
| D | LYS352 |
| D | LEU468 |
| D | SER471 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue K C 505 |
| Chain | Residue |
| C | GLY303 |
| C | GLY305 |
| C | CYS308 |
| D | GLU470 |
| D | SER471 |
| D | HIS472 |
| site_id | AD5 |
| Number of Residues | 25 |
| Details | binding site for residue IMP D 501 |
| Chain | Residue |
| D | ALA49 |
| D | MET51 |
| D | ASN280 |
| D | GLY305 |
| D | SER306 |
| D | ILE307 |
| D | CYS308 |
| D | ASP341 |
| D | GLY342 |
| D | GLY343 |
| D | MET362 |
| D | LEU363 |
| D | GLY364 |
| D | SER365 |
| D | TYR388 |
| D | GLY390 |
| D | MET391 |
| D | GLY392 |
| D | GLU416 |
| D | GLY417 |
| D | 8LA502 |
| D | HOH604 |
| D | HOH608 |
| D | HOH612 |
| D | HOH634 |
| site_id | AD6 |
| Number of Residues | 16 |
| Details | binding site for residue 8LA D 502 |
| Chain | Residue |
| B | LEU26 |
| B | ALA441 |
| B | GLY444 |
| D | THR252 |
| D | ALA253 |
| D | HIS254 |
| D | SER257 |
| D | GLY259 |
| D | VAL260 |
| D | THR310 |
| D | MET391 |
| D | GLY392 |
| D | VAL414 |
| D | GLU416 |
| D | IMP501 |
| D | HOH623 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue GOL D 503 |
| Chain | Residue |
| B | SER464 |
| D | ASP15 |
| D | ARG462 |
| site_id | AD8 |
| Number of Residues | 23 |
| Details | binding site for residue IMP E 501 |
| Chain | Residue |
| E | ALA49 |
| E | MET51 |
| E | ASN280 |
| E | GLY305 |
| E | SER306 |
| E | ILE307 |
| E | CYS308 |
| E | ASP341 |
| E | GLY342 |
| E | GLY343 |
| E | MET362 |
| E | LEU363 |
| E | GLY364 |
| E | SER365 |
| E | TYR388 |
| E | GLY390 |
| E | MET391 |
| E | GLY392 |
| E | GLU416 |
| E | GLY417 |
| E | 8LA502 |
| E | HOH604 |
| E | HOH624 |
| site_id | AD9 |
| Number of Residues | 17 |
| Details | binding site for residue 8LA E 502 |
| Chain | Residue |
| E | VAL229 |
| E | THR252 |
| E | ALA253 |
| E | HIS254 |
| E | SER257 |
| E | GLY259 |
| E | VAL260 |
| E | THR310 |
| E | MET391 |
| E | GLY392 |
| E | VAL414 |
| E | GLU416 |
| E | IMP501 |
| E | HOH628 |
| G | ALA441 |
| G | GLY444 |
| G | TYR445 |
| site_id | AE1 |
| Number of Residues | 7 |
| Details | binding site for residue K E 503 |
| Chain | Residue |
| E | GLU470 |
| E | SER471 |
| E | HIS472 |
| F | GLY303 |
| F | PRO304 |
| F | GLY305 |
| F | CYS308 |
| site_id | AE2 |
| Number of Residues | 1 |
| Details | binding site for residue PEG E 504 |
| Chain | Residue |
| E | ASN296 |
| site_id | AE3 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 E 505 |
| Chain | Residue |
| E | THR322 |
| E | ASP326 |
| F | PHE6 |
| site_id | AE4 |
| Number of Residues | 6 |
| Details | binding site for residue K E 506 |
| Chain | Residue |
| E | GLY303 |
| E | GLY305 |
| E | CYS308 |
| G | GLU470 |
| G | SER471 |
| G | HIS472 |
| site_id | AE5 |
| Number of Residues | 20 |
| Details | binding site for residue IMP F 500 |
| Chain | Residue |
| F | ALA49 |
| F | MET51 |
| F | ASN280 |
| F | GLY305 |
| F | SER306 |
| F | ILE307 |
| F | CYS308 |
| F | ASP341 |
| F | GLY343 |
| F | MET362 |
| F | GLY364 |
| F | SER365 |
| F | TYR388 |
| F | GLY390 |
| F | MET391 |
| F | GLY392 |
| F | GLU416 |
| F | GLY417 |
| F | 8LA501 |
| F | HOH607 |
| site_id | AE6 |
| Number of Residues | 16 |
| Details | binding site for residue 8LA F 501 |
| Chain | Residue |
| E | PRO27 |
| E | GLY444 |
| E | TYR445 |
| F | VAL229 |
| F | THR252 |
| F | ALA253 |
| F | HIS254 |
| F | SER257 |
| F | GLY259 |
| F | VAL260 |
| F | THR310 |
| F | MET391 |
| F | GLY392 |
| F | VAL414 |
| F | GLU416 |
| F | IMP500 |
| site_id | AE7 |
| Number of Residues | 6 |
| Details | binding site for residue K F 502 |
| Chain | Residue |
| F | GLU470 |
| F | SER471 |
| F | HIS472 |
| H | GLY303 |
| H | GLY305 |
| H | CYS308 |
| site_id | AE8 |
| Number of Residues | 22 |
| Details | binding site for residue IMP G 500 |
| Chain | Residue |
| G | ALA49 |
| G | MET51 |
| G | ASN280 |
| G | GLY305 |
| G | SER306 |
| G | ILE307 |
| G | CYS308 |
| G | ASP341 |
| G | GLY342 |
| G | GLY343 |
| G | MET362 |
| G | LEU363 |
| G | GLY364 |
| G | SER365 |
| G | TYR388 |
| G | GLY390 |
| G | MET391 |
| G | GLY392 |
| G | GLU416 |
| G | GLY417 |
| G | 8LA501 |
| G | HOH612 |
| site_id | AE9 |
| Number of Residues | 14 |
| Details | binding site for residue 8LA G 501 |
| Chain | Residue |
| G | THR252 |
| G | ALA253 |
| G | HIS254 |
| G | SER257 |
| G | GLY259 |
| G | VAL260 |
| G | MET391 |
| G | GLY392 |
| G | GLU416 |
| G | IMP500 |
| H | LEU26 |
| H | ALA441 |
| H | GLY444 |
| H | TYR445 |
| site_id | AF1 |
| Number of Residues | 6 |
| Details | binding site for residue K G 502 |
| Chain | Residue |
| G | GLY303 |
| G | GLY305 |
| G | CYS308 |
| H | GLU470 |
| H | SER471 |
| H | HIS472 |
| site_id | AF2 |
| Number of Residues | 19 |
| Details | binding site for residue IMP H 500 |
| Chain | Residue |
| H | ALA49 |
| H | MET51 |
| H | GLY305 |
| H | SER306 |
| H | ILE307 |
| H | CYS308 |
| H | ASP341 |
| H | GLY343 |
| H | MET362 |
| H | LEU363 |
| H | GLY364 |
| H | SER365 |
| H | TYR388 |
| H | GLY390 |
| H | MET391 |
| H | GLY392 |
| H | GLU416 |
| H | GLY417 |
| H | 8LA501 |
| site_id | AF3 |
| Number of Residues | 15 |
| Details | binding site for residue 8LA H 501 |
| Chain | Residue |
| F | PRO27 |
| F | ALA441 |
| F | GLY444 |
| F | TYR445 |
| H | VAL229 |
| H | THR252 |
| H | ALA253 |
| H | HIS254 |
| H | SER257 |
| H | GLY259 |
| H | VAL260 |
| H | MET391 |
| H | GLY392 |
| H | GLU416 |
| H | IMP500 |
Functional Information from PROSITE/UniProt
| site_id | PS00487 |
| Number of Residues | 13 |
| Details | IMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. VKVGIGpGSICtT |
| Chain | Residue | Details |
| A | VAL298-THR310 |
