4MY9
Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase with an Internal Deletion of the CBS Domain from Bacillus anthracis str. Ames complexed with inhibitor C91
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 | ALA49 |
| A | SER365 |
| A | TYR388 |
| A | GLY390 |
| A | MET391 |
| A | GLY392 |
| A | GLU416 |
| A | GLY417 |
| A | C91501 |
| A | HOH601 |
| A | HOH612 |
| A | MET51 |
| A | HOH613 |
| A | GLY305 |
| A | SER306 |
| A | CYS308 |
| A | ASP341 |
| A | GLY342 |
| A | GLY343 |
| A | GLY364 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE C91 A 501 |
| Chain | Residue |
| A | ALA253 |
| A | GLY392 |
| A | MET397 |
| A | LEU413 |
| A | GLU416 |
| A | IMP500 |
| C | ALA441 |
| C | GLY444 |
| C | TYR445 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MLI A 502 |
| Chain | Residue |
| A | GLU9 |
| A | THR322 |
| A | HOH630 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE IMP B 500 |
| Chain | Residue |
| B | ALA49 |
| B | MET51 |
| B | GLY305 |
| B | SER306 |
| B | ILE307 |
| B | CYS308 |
| B | THR310 |
| B | ASP341 |
| B | GLY342 |
| B | GLY343 |
| B | GLY364 |
| B | SER365 |
| B | TYR388 |
| B | GLY390 |
| B | MET391 |
| B | GLY392 |
| B | GLU416 |
| B | GLY417 |
| B | C91501 |
| B | HOH602 |
| B | HOH607 |
| B | HOH614 |
| B | HOH623 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE C91 B 501 |
| Chain | Residue |
| A | PRO27 |
| A | ALA441 |
| A | GLY444 |
| A | TYR445 |
| B | ALA253 |
| B | MET391 |
| B | MET397 |
| B | LEU413 |
| B | GLU416 |
| B | IMP500 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MLI B 502 |
| Chain | Residue |
| B | GLU9 |
| B | THR322 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MLI B 503 |
| Chain | Residue |
| B | SER37 |
| B | GLU38 |
| B | SER39 |
| B | ARG268 |
| B | PRO272 |
| B | SER273 |
| B | ASN275 |
| B | ASN296 |
| B | HOH643 |
| site_id | AC8 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE IMP C 500 |
| Chain | Residue |
| C | ALA49 |
| C | MET51 |
| C | GLY305 |
| C | SER306 |
| C | ILE307 |
| C | CYS308 |
| C | ASP341 |
| C | GLY342 |
| C | GLY343 |
| C | MET362 |
| C | GLY364 |
| C | SER365 |
| C | TYR388 |
| C | GLY390 |
| C | MET391 |
| C | GLY392 |
| C | GLU416 |
| C | C91501 |
| C | HOH602 |
| C | HOH617 |
| C | HOH618 |
| C | HOH621 |
| C | HOH628 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE C91 C 501 |
| Chain | Residue |
| C | ALA253 |
| C | MET391 |
| C | MET397 |
| C | LEU413 |
| C | GLU416 |
| C | IMP500 |
| D | VAL25 |
| D | PRO27 |
| D | ALA441 |
| D | GLY444 |
| D | TYR445 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MLI C 502 |
| Chain | Residue |
| C | SER37 |
| C | GLU38 |
| C | SER39 |
| C | ARG268 |
| C | PRO272 |
| C | SER273 |
| C | LEU274 |
| C | ASN275 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MLI C 503 |
| Chain | Residue |
| A | PHE6 |
| C | GLU9 |
| C | THR322 |
| C | ASP326 |
| site_id | BC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE IMP D 500 |
| Chain | Residue |
| D | ALA49 |
| D | MET51 |
| D | GLY305 |
| D | SER306 |
| D | ILE307 |
| D | CYS308 |
| D | ASP341 |
| D | GLY342 |
| D | GLY343 |
| D | GLY364 |
| D | SER365 |
| D | TYR388 |
| D | GLY390 |
| D | MET391 |
| D | GLY392 |
| D | GLU416 |
| D | GLY417 |
| D | C91501 |
| D | HOH601 |
| D | HOH602 |
| D | HOH616 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE C91 D 501 |
| Chain | Residue |
| B | ALA441 |
| B | GLY444 |
| B | TYR445 |
| D | ALA253 |
| D | MET397 |
| D | GLU416 |
| D | IMP500 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MLI D 502 |
| Chain | Residue |
| D | GLU9 |
| D | LEU11 |
| D | THR322 |
| D | HOH618 |
| site_id | BC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE IMP E 500 |
| Chain | Residue |
| E | ALA49 |
| E | MET51 |
| E | ASN280 |
| E | GLY305 |
| E | SER306 |
| E | CYS308 |
| E | ASP341 |
| E | GLY342 |
| E | GLY343 |
| E | MET362 |
| E | GLY364 |
| E | SER365 |
| E | TYR388 |
| E | GLY390 |
| E | MET391 |
| E | GLY392 |
| E | GLU416 |
| E | GLY417 |
| E | C91501 |
| E | HOH606 |
| E | HOH608 |
| E | HOH618 |
| E | HOH630 |
| site_id | BC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE C91 E 501 |
| Chain | Residue |
| E | ALA253 |
| E | THR310 |
| E | MET391 |
| E | GLY392 |
| E | MET397 |
| E | GLU416 |
| E | IMP500 |
| E | HOH617 |
| F | ALA441 |
| F | GLY444 |
| F | TYR445 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MLI E 502 |
| Chain | Residue |
| E | GLU9 |
| E | THR322 |
| E | ASP326 |
| site_id | BC9 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE IMP F 500 |
| Chain | Residue |
| F | ALA49 |
| F | MET51 |
| F | ASN280 |
| F | GLY305 |
| F | SER306 |
| F | CYS308 |
| F | ASP341 |
| F | GLY342 |
| F | GLY343 |
| F | MET362 |
| F | GLY364 |
| F | SER365 |
| F | TYR388 |
| F | GLY390 |
| F | MET391 |
| F | GLY392 |
| F | GLU416 |
| F | GLY417 |
| F | C91501 |
| F | HOH601 |
| F | HOH610 |
| site_id | CC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE C91 F 501 |
| Chain | Residue |
| F | ALA253 |
| F | MET391 |
| F | MET397 |
| F | GLU416 |
| F | IMP500 |
| H | ALA441 |
| H | GLY444 |
| H | TYR445 |
| site_id | CC2 |
| Number of Residues | 23 |
| 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 | GLY364 |
| G | SER365 |
| G | TYR388 |
| G | GLY390 |
| G | MET391 |
| G | GLY392 |
| G | GLU416 |
| G | GLY417 |
| G | C91501 |
| G | HOH606 |
| G | HOH614 |
| G | HOH627 |
| G | HOH628 |
| site_id | CC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE C91 G 501 |
| Chain | Residue |
| E | PRO27 |
| E | ALA441 |
| E | GLY444 |
| G | ALA253 |
| G | MET397 |
| G | GLU416 |
| G | IMP500 |
| G | HOH624 |
| site_id | CC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MLI G 502 |
| Chain | Residue |
| G | GLU9 |
| G | LEU11 |
| G | THR322 |
| site_id | CC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE IMP H 500 |
| Chain | Residue |
| H | ALA49 |
| H | MET51 |
| H | ASN280 |
| H | GLY305 |
| H | SER306 |
| H | ILE307 |
| H | CYS308 |
| H | ASP341 |
| H | GLY342 |
| H | GLY343 |
| H | MET362 |
| H | GLY364 |
| H | SER365 |
| H | TYR388 |
| H | GLY390 |
| H | MET391 |
| H | GLY392 |
| H | GLU416 |
| H | GLY417 |
| H | C91501 |
| H | HOH609 |
| H | HOH610 |
| H | HOH611 |
| site_id | CC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE C91 H 501 |
| Chain | Residue |
| G | ALA441 |
| G | GLY444 |
| G | TYR445 |
| H | ALA253 |
| H | MET391 |
| H | MET397 |
| H | LEU413 |
| H | GLU416 |
| H | IMP500 |
| H | HOH612 |
| site_id | CC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MLI H 502 |
| Chain | Residue |
| F | PHE6 |
| H | GLU9 |
| H | THR322 |
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 |
