5URQ
Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Campylobacter jejuni in the complex with inhibitor p176
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 501 |
| Chain | Residue |
| A | ALA46 |
| A | GLY336 |
| A | MET355 |
| A | GLY357 |
| A | SER358 |
| A | TYR381 |
| A | GLY383 |
| A | MET384 |
| A | GLY385 |
| A | GLU411 |
| A | GLY412 |
| A | MET48 |
| A | 8L7502 |
| A | ASN273 |
| A | GLY298 |
| A | SER299 |
| A | ILE300 |
| A | CYS301 |
| A | ASP334 |
| A | GLY335 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue 8L7 A 502 |
| Chain | Residue |
| A | VAL224 |
| A | SER245 |
| A | ALA246 |
| A | HIS247 |
| A | SER250 |
| A | GLY252 |
| A | THR303 |
| A | GLY385 |
| A | GLU411 |
| A | IMP501 |
| D | GLY439 |
| D | TYR440 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue K A 503 |
| Chain | Residue |
| A | GLY296 |
| A | GLY298 |
| A | CYS301 |
| D | GLU465 |
| D | SER466 |
| D | HIS467 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue K A 504 |
| Chain | Residue |
| A | GLU465 |
| A | SER466 |
| A | HIS467 |
| B | GLY296 |
| B | GLY298 |
| B | CYS301 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | binding site for residue IMP B 500 |
| Chain | Residue |
| B | MET48 |
| B | ASN273 |
| B | GLY298 |
| B | SER299 |
| B | ILE300 |
| B | CYS301 |
| B | ASP334 |
| B | GLY335 |
| B | GLY336 |
| B | MET355 |
| B | GLY357 |
| B | SER358 |
| B | TYR381 |
| B | GLY383 |
| B | MET384 |
| B | GLY385 |
| B | GLU411 |
| B | GLY412 |
| B | 8L7501 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue 8L7 B 501 |
| Chain | Residue |
| A | GLY439 |
| A | TYR440 |
| B | VAL224 |
| B | SER245 |
| B | ALA246 |
| B | HIS247 |
| B | SER250 |
| B | GLY252 |
| B | MET384 |
| B | GLY385 |
| B | GLU411 |
| B | IMP500 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue K B 502 |
| Chain | Residue |
| B | GLU465 |
| B | SER466 |
| B | HIS467 |
| C | GLY296 |
| C | GLY298 |
| C | CYS301 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | binding site for residue IMP C 500 |
| Chain | Residue |
| C | MET48 |
| C | ASN273 |
| C | GLY298 |
| C | SER299 |
| C | ILE300 |
| C | CYS301 |
| C | ASP334 |
| C | GLY335 |
| C | GLY336 |
| C | MET355 |
| C | GLY357 |
| C | SER358 |
| C | TYR381 |
| C | GLY383 |
| C | MET384 |
| C | GLY385 |
| C | GLU411 |
| C | 8L7501 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | binding site for residue 8L7 C 501 |
| Chain | Residue |
| B | SER20 |
| B | SER436 |
| B | GLY439 |
| B | TYR440 |
| C | VAL224 |
| C | SER245 |
| C | ALA246 |
| C | HIS247 |
| C | SER250 |
| C | GLY252 |
| C | ILE253 |
| C | MET384 |
| C | GLY385 |
| C | MET390 |
| C | GLU411 |
| C | IMP500 |
| site_id | AD1 |
| Number of Residues | 18 |
| Details | binding site for residue IMP D 500 |
| Chain | Residue |
| D | ALA46 |
| D | MET48 |
| D | ASN273 |
| D | GLY298 |
| D | SER299 |
| D | ILE300 |
| D | CYS301 |
| D | ASP334 |
| D | GLY335 |
| D | GLY336 |
| D | GLY357 |
| D | SER358 |
| D | TYR381 |
| D | GLY383 |
| D | MET384 |
| D | GLY385 |
| D | GLU411 |
| D | 8L7501 |
| site_id | AD2 |
| Number of Residues | 13 |
| Details | binding site for residue 8L7 D 501 |
| Chain | Residue |
| C | SER436 |
| C | GLY439 |
| C | TYR440 |
| D | VAL224 |
| D | SER245 |
| D | ALA246 |
| D | HIS247 |
| D | SER250 |
| D | GLY252 |
| D | ILE253 |
| D | GLY385 |
| D | GLU411 |
| D | IMP500 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue K D 502 |
| Chain | Residue |
| C | GLU465 |
| C | SER466 |
| C | HIS467 |
| D | GLY296 |
| D | GLY298 |
| D | CYS301 |
| site_id | AD4 |
| Number of Residues | 19 |
| Details | binding site for residue IMP E 501 |
| Chain | Residue |
| E | ALA46 |
| E | MET48 |
| E | ASN273 |
| E | GLY298 |
| E | SER299 |
| E | ILE300 |
| E | CYS301 |
| E | ASP334 |
| E | GLY336 |
| E | MET355 |
| E | GLY357 |
| E | SER358 |
| E | TYR381 |
| E | GLY383 |
| E | MET384 |
| E | GLY385 |
| E | GLU411 |
| E | GLY412 |
| E | 8L7502 |
| site_id | AD5 |
| Number of Residues | 12 |
| Details | binding site for residue 8L7 E 502 |
| Chain | Residue |
| E | SER245 |
| E | ALA246 |
| E | HIS247 |
| E | SER250 |
| E | THR303 |
| E | MET384 |
| E | GLY385 |
| E | GLU411 |
| E | IMP501 |
| H | LEU23 |
| H | SER436 |
| H | GLY439 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue K E 503 |
| Chain | Residue |
| E | GLY296 |
| E | GLY298 |
| E | CYS301 |
| H | GLU465 |
| H | SER466 |
| H | HIS467 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue K E 504 |
| Chain | Residue |
| E | GLU465 |
| E | SER466 |
| E | HIS467 |
| F | GLY296 |
| F | GLY298 |
| F | CYS301 |
| site_id | AD8 |
| Number of Residues | 17 |
| Details | binding site for residue IMP F 500 |
| Chain | Residue |
| F | ASN273 |
| F | GLY298 |
| F | SER299 |
| F | ILE300 |
| F | CYS301 |
| F | ASP334 |
| F | GLY336 |
| F | MET355 |
| F | GLY357 |
| F | SER358 |
| F | TYR381 |
| F | GLY383 |
| F | MET384 |
| F | GLY385 |
| F | GLU411 |
| F | GLY412 |
| F | 8L7501 |
| site_id | AD9 |
| Number of Residues | 11 |
| Details | binding site for residue 8L7 F 501 |
| Chain | Residue |
| E | GLY439 |
| E | TYR440 |
| F | VAL224 |
| F | SER245 |
| F | ALA246 |
| F | HIS247 |
| F | SER250 |
| F | THR303 |
| F | MET384 |
| F | GLU411 |
| F | IMP500 |
| site_id | AE1 |
| Number of Residues | 6 |
| Details | binding site for residue K F 502 |
| Chain | Residue |
| F | GLU465 |
| F | SER466 |
| F | HIS467 |
| G | GLY296 |
| G | GLY298 |
| G | CYS301 |
| site_id | AE2 |
| Number of Residues | 20 |
| Details | binding site for residue IMP H 500 |
| Chain | Residue |
| H | ALA46 |
| H | MET48 |
| H | ASN273 |
| H | GLY298 |
| H | SER299 |
| H | ILE300 |
| H | CYS301 |
| H | ASP334 |
| H | GLY335 |
| H | GLY336 |
| H | MET355 |
| H | GLY357 |
| H | SER358 |
| H | TYR381 |
| H | GLY383 |
| H | MET384 |
| H | GLY385 |
| H | GLU411 |
| H | GLY412 |
| H | 8L7501 |
| site_id | AE3 |
| Number of Residues | 11 |
| Details | binding site for residue 8L7 H 501 |
| Chain | Residue |
| G | GLY439 |
| G | TYR440 |
| H | SER245 |
| H | ALA246 |
| H | HIS247 |
| H | SER250 |
| H | GLY252 |
| H | GLY385 |
| H | MET390 |
| H | GLU411 |
| H | IMP500 |
| site_id | AE4 |
| Number of Residues | 6 |
| Details | binding site for residue K G 501 |
| Chain | Residue |
| G | GLU465 |
| G | SER466 |
| G | HIS467 |
| H | GLY296 |
| H | GLY298 |
| H | CYS301 |
| site_id | AE5 |
| Number of Residues | 19 |
| Details | binding site for residue IMP G 502 |
| Chain | Residue |
| G | ALA46 |
| G | MET48 |
| G | ASN273 |
| G | GLY298 |
| G | SER299 |
| G | ILE300 |
| G | CYS301 |
| G | ASP334 |
| G | GLY335 |
| G | GLY336 |
| G | GLY357 |
| G | SER358 |
| G | TYR381 |
| G | GLY383 |
| G | MET384 |
| G | GLY385 |
| G | GLU411 |
| G | GLY412 |
| G | 8L7503 |
| site_id | AE6 |
| Number of Residues | 12 |
| Details | binding site for residue 8L7 G 503 |
| Chain | Residue |
| F | SER436 |
| F | GLY439 |
| F | TYR440 |
| G | VAL224 |
| G | ALA246 |
| G | SER250 |
| G | GLY252 |
| G | MET384 |
| G | GLY385 |
| G | MET390 |
| G | GLU411 |
| G | IMP502 |
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 | VAL291-THR303 |
