4Q33
Crystal Structure of Inosine 5'-monophosphate Dehydrogenase from Clostridium perfringens Complexed with IMP and A110
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 | 20 |
| Details | BINDING SITE FOR RESIDUE IMP A 500 |
| Chain | Residue |
| A | ALA47 |
| A | SER360 |
| A | TYR383 |
| A | GLY385 |
| A | MET386 |
| A | GLY387 |
| A | SER388 |
| A | GLU411 |
| A | GLY412 |
| A | 2YA501 |
| A | HOH603 |
| A | MET49 |
| A | HOH604 |
| A | SER301 |
| A | ILE302 |
| A | CYS303 |
| A | ASP336 |
| A | GLY337 |
| A | GLY338 |
| A | GLY359 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 2YA A 501 |
| Chain | Residue |
| A | ALA248 |
| A | HIS249 |
| A | GLY387 |
| A | VAL409 |
| A | GLU411 |
| A | IMP500 |
| C | PRO25 |
| C | SER436 |
| C | GLY439 |
| C | TYR440 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE IMP B 501 |
| Chain | Residue |
| B | ALA47 |
| B | MET49 |
| B | GLY300 |
| B | SER301 |
| B | ILE302 |
| B | CYS303 |
| B | ASP336 |
| B | GLY337 |
| B | GLY338 |
| B | MET358 |
| B | GLY359 |
| B | SER360 |
| B | TYR383 |
| B | GLY385 |
| B | MET386 |
| B | GLY387 |
| B | GLU411 |
| B | 2YA502 |
| B | HOH613 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 2YA B 502 |
| Chain | Residue |
| A | PRO25 |
| A | GLY439 |
| B | ALA248 |
| B | HIS249 |
| B | THR305 |
| B | MET386 |
| B | GLY387 |
| B | MET392 |
| B | PHE408 |
| B | VAL409 |
| B | GLU411 |
| B | IMP501 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 2YA B 503 |
| Chain | Residue |
| B | GLY439 |
| B | TYR440 |
| D | ALA248 |
| D | VAL409 |
| D | GLU411 |
| D | IMP501 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE IMP C 500 |
| Chain | Residue |
| C | ALA47 |
| C | MET49 |
| C | GLY300 |
| C | SER301 |
| C | ILE302 |
| C | CYS303 |
| C | ASP336 |
| C | GLY337 |
| C | GLY338 |
| C | MET358 |
| C | GLY359 |
| C | SER360 |
| C | TYR383 |
| C | GLY385 |
| C | MET386 |
| C | GLY387 |
| C | GLU411 |
| C | GLY412 |
| C | 2YA501 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 2YA C 501 |
| Chain | Residue |
| C | ASP246 |
| C | GLY387 |
| C | MET392 |
| C | PHE408 |
| C | VAL409 |
| C | GLU411 |
| C | IMP500 |
| D | SER436 |
| D | GLY439 |
| D | TYR440 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE IMP D 501 |
| Chain | Residue |
| D | ASN275 |
| D | GLY300 |
| D | SER301 |
| D | ILE302 |
| D | CYS303 |
| D | ASP336 |
| D | GLY337 |
| D | GLY338 |
| D | MET357 |
| D | GLY359 |
| D | SER360 |
| D | TYR383 |
| D | GLY385 |
| D | MET386 |
| D | GLY387 |
| D | GLU411 |
| D | HOH606 |
| B | 2YA503 |
| D | ALA47 |
| D | MET49 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY D 502 |
| Chain | Residue |
| D | LYS420 |
| D | THR426 |
| D | PRO478 |
| site_id | BC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE IMP E 500 |
| Chain | Residue |
| E | MET49 |
| E | GLY300 |
| E | SER301 |
| E | ILE302 |
| E | CYS303 |
| E | ASP336 |
| E | GLY337 |
| E | GLY338 |
| E | GLY359 |
| E | SER360 |
| E | TYR383 |
| E | GLY385 |
| E | MET386 |
| E | GLY387 |
| E | GLU411 |
| E | GLY412 |
| E | 2YA501 |
| E | HOH617 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 2YA E 501 |
| Chain | Residue |
| E | MET386 |
| E | PHE408 |
| E | VAL409 |
| E | GLU411 |
| E | IMP500 |
| G | PRO25 |
| G | GLY439 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT E 502 |
| Chain | Residue |
| E | THR32 |
| E | LYS327 |
| E | GLU447 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 E 503 |
| Chain | Residue |
| E | ASN26 |
| site_id | BC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE IMP F 500 |
| Chain | Residue |
| F | ALA47 |
| F | MET49 |
| F | GLY300 |
| F | SER301 |
| F | ILE302 |
| F | CYS303 |
| F | ASP336 |
| F | GLY338 |
| F | GLY359 |
| F | SER360 |
| F | TYR383 |
| F | GLY385 |
| F | MET386 |
| F | GLY387 |
| F | GLU411 |
| F | GLY412 |
| F | 2YA501 |
| F | HOH613 |
| F | HOH615 |
| site_id | BC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 2YA F 501 |
| Chain | Residue |
| E | PRO25 |
| E | SER436 |
| E | GLY439 |
| E | TYR440 |
| F | ALA248 |
| F | MET386 |
| F | GLY387 |
| F | VAL409 |
| F | GLU411 |
| F | IMP500 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT F 502 |
| Chain | Residue |
| E | ALA461 |
| E | ARG464 |
| F | ASP12 |
| F | THR459 |
| F | SER460 |
| F | PHE463 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL F 503 |
| Chain | Residue |
| F | THR32 |
| F | LYS327 |
| F | LEU349 |
| F | GLY352 |
| F | CYS354 |
| F | GLU447 |
| F | TYR450 |
| site_id | BC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT F 504 |
| Chain | Residue |
| F | PHE408 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT F 505 |
| Chain | Residue |
| F | ALA277 |
| F | ASP321 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL F 506 |
| Chain | Residue |
| F | LYS340 |
| F | TYR341 |
| F | SER342 |
| F | ASN479 |
| site_id | CC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE IMP G 500 |
| Chain | Residue |
| G | ALA47 |
| G | MET49 |
| G | GLY300 |
| G | SER301 |
| G | ILE302 |
| G | CYS303 |
| G | ASP336 |
| G | GLY337 |
| G | GLY338 |
| G | GLY359 |
| G | SER360 |
| G | TYR383 |
| G | GLY385 |
| G | MET386 |
| G | GLY387 |
| G | SER388 |
| G | GLU411 |
| G | GLY412 |
| G | 2YA501 |
| site_id | CC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 2YA G 501 |
| Chain | Residue |
| G | ALA248 |
| G | MET386 |
| G | GLY387 |
| G | PHE408 |
| G | VAL409 |
| G | GLU411 |
| G | IMP500 |
| G | FMT502 |
| G | HOH605 |
| H | GLY439 |
| H | TYR440 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT G 502 |
| Chain | Residue |
| G | THR247 |
| G | ALA248 |
| G | HIS249 |
| G | SER252 |
| G | 2YA501 |
| G | HOH605 |
| site_id | CC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE IMP H 500 |
| Chain | Residue |
| H | ALA47 |
| H | MET49 |
| H | GLY300 |
| H | SER301 |
| H | ILE302 |
| H | CYS303 |
| H | ASP336 |
| H | GLY337 |
| H | GLY338 |
| H | MET358 |
| H | GLY359 |
| H | SER360 |
| H | TYR383 |
| H | GLY385 |
| H | MET386 |
| H | GLY387 |
| H | GLU411 |
| H | GLY412 |
| H | 2YA501 |
| H | HOH606 |
| site_id | CC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 2YA H 501 |
| Chain | Residue |
| F | GLY439 |
| H | ALA248 |
| H | HIS249 |
| H | MET386 |
| H | GLY387 |
| H | MET392 |
| H | GLU411 |
| H | IMP500 |
| H | HOH617 |
| site_id | CC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT H 502 |
| Chain | Residue |
| H | LYS327 |
| H | GLY352 |
| H | ALA353 |
| H | GLU447 |
| site_id | CC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT H 503 |
| Chain | Residue |
| H | ALA277 |
| H | ASP321 |
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 | VAL293-THR305 |
