5UQG
Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Campylobacter jejuni in the complex with inhibitor p200
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 | 24 |
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 | 8L4502 |
A | HOH605 |
A | HOH612 |
A | HOH635 |
A | HOH680 |
A | ASN273 |
A | GLY298 |
A | SER299 |
A | ILE300 |
A | CYS301 |
A | ASP334 |
A | GLY335 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue 8L4 A 502 |
Chain | Residue |
A | ALA246 |
A | THR303 |
A | MET384 |
A | GLY385 |
A | MET390 |
A | VAL409 |
A | GLU411 |
A | IMP501 |
A | HOH642 |
B | PRO24 |
B | SER436 |
B | GLY439 |
B | TYR440 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | ARG16 |
A | PRO17 |
A | VAL441 |
A | ARG452 |
A | ALA453 |
A | GLU454 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue K A 504 |
Chain | Residue |
A | GLU465 |
A | SER466 |
A | HIS467 |
D | GLY296 |
D | GLY298 |
D | CYS301 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue K B 501 |
Chain | Residue |
A | GLY296 |
A | GLY298 |
A | CYS301 |
B | GLU465 |
B | SER466 |
B | HIS467 |
site_id | AC6 |
Number of Residues | 24 |
Details | binding site for residue IMP B 502 |
Chain | Residue |
B | ALA46 |
B | MET48 |
B | ASN273 |
B | GLY298 |
B | SER299 |
B | ILE300 |
B | CYS301 |
B | ASP334 |
B | GLY336 |
B | MET355 |
B | GLY357 |
B | SER358 |
B | TYR381 |
B | GLY383 |
B | MET384 |
B | GLY385 |
B | GLU411 |
B | GLY412 |
B | 8L4503 |
B | HOH606 |
B | HOH609 |
B | HOH623 |
B | HOH675 |
B | HOH682 |
site_id | AC7 |
Number of Residues | 14 |
Details | binding site for residue 8L4 B 503 |
Chain | Residue |
B | ALA246 |
B | THR303 |
B | MET384 |
B | GLY385 |
B | LEU408 |
B | VAL409 |
B | GLU411 |
B | IMP502 |
B | HOH610 |
H | PRO24 |
H | SER436 |
H | GLY439 |
H | TYR440 |
H | HOH662 |
site_id | AC8 |
Number of Residues | 25 |
Details | binding site for residue IMP C 500 |
Chain | Residue |
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 | GLY412 |
C | 8L4501 |
C | HOH601 |
C | HOH616 |
C | HOH623 |
C | HOH644 |
C | HOH646 |
C | ALA46 |
C | MET48 |
C | ASN273 |
C | GLY298 |
C | SER299 |
C | ILE300 |
site_id | AC9 |
Number of Residues | 11 |
Details | binding site for residue 8L4 C 501 |
Chain | Residue |
C | ALA246 |
C | THR303 |
C | MET384 |
C | GLY385 |
C | MET390 |
C | GLU411 |
C | IMP500 |
G | PRO24 |
G | SER436 |
G | GLY439 |
G | TYR440 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue K C 502 |
Chain | Residue |
C | GLU465 |
C | SER466 |
C | HIS467 |
E | GLY296 |
E | GLY298 |
E | CYS301 |
site_id | AD2 |
Number of Residues | 25 |
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 | MET355 |
D | GLY357 |
D | SER358 |
D | TYR381 |
D | GLY383 |
D | MET384 |
D | GLY385 |
D | GLU411 |
D | GLY412 |
D | 8L4501 |
D | HOH610 |
D | HOH623 |
D | HOH628 |
D | HOH651 |
D | HOH673 |
site_id | AD3 |
Number of Residues | 11 |
Details | binding site for residue 8L4 D 501 |
Chain | Residue |
A | SER436 |
A | GLY439 |
A | TYR440 |
A | HOH653 |
D | ALA246 |
D | THR303 |
D | MET384 |
D | GLY385 |
D | VAL409 |
D | GLU411 |
D | IMP500 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue K D 502 |
Chain | Residue |
D | GLU465 |
D | SER466 |
D | HIS467 |
H | GLY296 |
H | GLY298 |
H | CYS301 |
site_id | AD5 |
Number of Residues | 25 |
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 | GLY335 |
E | GLY336 |
E | MET355 |
E | GLY357 |
E | SER358 |
E | TYR381 |
E | GLY383 |
E | MET384 |
E | GLY385 |
E | GLU411 |
E | GLY412 |
E | 8L4502 |
E | HOH614 |
E | HOH637 |
E | HOH640 |
E | HOH646 |
E | HOH666 |
site_id | AD6 |
Number of Residues | 12 |
Details | binding site for residue 8L4 E 502 |
Chain | Residue |
C | PRO24 |
C | SER436 |
C | GLY439 |
C | TYR440 |
C | HOH643 |
E | ALA246 |
E | HIS247 |
E | THR303 |
E | MET384 |
E | GLY385 |
E | GLU411 |
E | IMP501 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue EDO E 503 |
Chain | Residue |
E | ARG16 |
E | PRO17 |
E | VAL441 |
E | ARG452 |
E | ALA453 |
E | GLU454 |
site_id | AD8 |
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 | AD9 |
Number of Residues | 24 |
Details | binding site for residue IMP F 501 |
Chain | Residue |
F | ALA46 |
F | MET48 |
F | ASN273 |
F | GLY298 |
F | SER299 |
F | ILE300 |
F | CYS301 |
F | ASP334 |
F | GLY335 |
F | GLY336 |
F | MET355 |
F | GLY357 |
F | SER358 |
F | TYR381 |
F | GLY383 |
F | MET384 |
F | GLY385 |
F | GLU411 |
F | GLY412 |
F | 8L4502 |
F | HOH601 |
F | HOH605 |
F | HOH615 |
F | HOH629 |
site_id | AE1 |
Number of Residues | 13 |
Details | binding site for residue 8L4 F 502 |
Chain | Residue |
E | VAL22 |
E | SER436 |
E | GLY439 |
E | TYR440 |
F | ALA246 |
F | THR303 |
F | MET384 |
F | GLY385 |
F | LEU408 |
F | VAL409 |
F | GLU411 |
F | IMP501 |
F | HOH670 |
site_id | AE2 |
Number of Residues | 9 |
Details | binding site for residue 8L4 F 503 |
Chain | Residue |
F | SER436 |
F | GLY439 |
F | TYR440 |
G | ALA246 |
G | THR303 |
G | GLY385 |
G | VAL409 |
G | GLU411 |
G | IMP502 |
site_id | AE3 |
Number of Residues | 6 |
Details | binding site for residue K F 504 |
Chain | Residue |
F | GLU465 |
F | SER466 |
F | HIS467 |
G | GLY296 |
G | GLY298 |
G | CYS301 |
site_id | AE4 |
Number of Residues | 6 |
Details | binding site for residue K G 501 |
Chain | Residue |
C | GLY296 |
C | GLY298 |
C | CYS301 |
G | GLU465 |
G | SER466 |
G | HIS467 |
site_id | AE5 |
Number of Residues | 25 |
Details | binding site for residue IMP G 502 |
Chain | Residue |
F | 8L4503 |
G | ALA46 |
G | MET48 |
G | ASN273 |
G | GLY298 |
G | SER299 |
G | ILE300 |
G | CYS301 |
G | ASP334 |
G | GLY335 |
G | GLY336 |
G | MET355 |
G | ILE356 |
G | GLY357 |
G | SER358 |
G | TYR381 |
G | GLY383 |
G | MET384 |
G | GLY385 |
G | GLU411 |
G | GLY412 |
G | HOH615 |
G | HOH636 |
G | HOH650 |
G | HOH655 |
site_id | AE6 |
Number of Residues | 6 |
Details | binding site for residue K H 501 |
Chain | Residue |
B | GLY296 |
B | GLY298 |
B | CYS301 |
H | GLU465 |
H | SER466 |
H | HIS467 |
site_id | AE7 |
Number of Residues | 25 |
Details | binding site for residue IMP H 502 |
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 | 8L4503 |
H | HOH608 |
H | HOH615 |
H | HOH624 |
H | HOH636 |
H | HOH655 |
site_id | AE8 |
Number of Residues | 11 |
Details | binding site for residue 8L4 H 503 |
Chain | Residue |
D | PRO24 |
D | SER436 |
D | GLY439 |
D | TYR440 |
H | ALA246 |
H | THR303 |
H | GLY385 |
H | VAL409 |
H | GLU411 |
H | IMP502 |
H | HOH671 |
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 |