5UQH
Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Campylobacter jejuni in the complex with inhibitor p182
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 | MET355 |
A | ILE356 |
A | GLY357 |
A | SER358 |
A | TYR381 |
A | GLY383 |
A | MET384 |
A | GLY385 |
A | GLU411 |
A | HOH606 |
A | ASN273 |
A | HOH614 |
A | HOH625 |
A | HOH642 |
A | HOH651 |
D | 8L1501 |
A | GLY298 |
A | SER299 |
A | ILE300 |
A | CYS301 |
A | ASP334 |
A | GLY335 |
A | GLY336 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue K A 502 |
Chain | Residue |
A | GLU465 |
A | SER466 |
A | HIS467 |
B | GLY296 |
B | GLY298 |
B | CYS301 |
site_id | AC3 |
Number of Residues | 26 |
Details | binding site for residue IMP B 500 |
Chain | Residue |
B | ALA46 |
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 | 8L1501 |
B | HOH604 |
B | HOH607 |
B | HOH609 |
B | HOH633 |
B | HOH644 |
B | HOH658 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue 8L1 B 501 |
Chain | Residue |
A | SER436 |
A | GLY439 |
A | TYR440 |
B | HIS247 |
B | THR303 |
B | MET384 |
B | GLY385 |
B | VAL409 |
B | GLU411 |
B | IMP500 |
site_id | AC5 |
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 | AC6 |
Number of Residues | 24 |
Details | binding site for residue IMP C 500 |
Chain | Residue |
C | ALA46 |
C | MET48 |
C | ASN273 |
C | GLY298 |
C | SER299 |
C | ILE300 |
C | CYS301 |
C | ASP334 |
C | GLY336 |
C | MET355 |
C | GLY357 |
C | SER358 |
C | TYR381 |
C | GLY383 |
C | MET384 |
C | GLY385 |
C | GLU411 |
C | GLY412 |
C | 8L1501 |
C | HOH614 |
C | HOH616 |
C | HOH620 |
C | HOH621 |
C | HOH641 |
site_id | AC7 |
Number of Residues | 11 |
Details | binding site for residue 8L1 C 501 |
Chain | Residue |
B | TYR440 |
C | VAL224 |
C | SER245 |
C | THR303 |
C | MET384 |
C | GLY385 |
C | GLU411 |
C | IMP500 |
B | LEU23 |
B | SER436 |
B | GLY439 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue K C 502 |
Chain | Residue |
C | GLU465 |
C | SER466 |
C | HIS467 |
D | GLY296 |
D | GLY298 |
D | CYS301 |
site_id | AC9 |
Number of Residues | 12 |
Details | binding site for residue 8L1 D 501 |
Chain | Residue |
A | ALA246 |
A | THR303 |
A | GLY385 |
A | MET390 |
A | GLU411 |
A | IMP501 |
A | HOH662 |
D | LEU23 |
D | SER436 |
D | GLY439 |
D | TYR440 |
D | HOH628 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue K D 502 |
Chain | Residue |
A | GLY296 |
A | GLY298 |
A | CYS301 |
D | GLU465 |
D | SER466 |
D | HIS467 |
site_id | AD2 |
Number of Residues | 24 |
Details | binding site for residue IMP D 503 |
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 | 8L1504 |
D | HOH602 |
D | HOH603 |
D | HOH611 |
D | HOH626 |
site_id | AD3 |
Number of Residues | 10 |
Details | binding site for residue 8L1 D 504 |
Chain | Residue |
C | SER436 |
C | GLY439 |
D | VAL224 |
D | SER245 |
D | ALA246 |
D | THR303 |
D | MET384 |
D | GLY385 |
D | GLU411 |
D | IMP503 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue EDO D 505 |
Chain | Residue |
D | ILE29 |
D | MET41 |
D | LEU63 |
D | ASP207 |
D | LEU431 |
D | ARG435 |
site_id | AD5 |
Number of Residues | 24 |
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 | 8L1502 |
E | HOH621 |
E | HOH629 |
E | HOH647 |
E | HOH651 |
site_id | AD6 |
Number of Residues | 11 |
Details | binding site for residue 8L1 E 502 |
Chain | Residue |
E | HIS247 |
E | THR303 |
E | MET384 |
E | GLY385 |
E | MET390 |
E | GLU411 |
E | IMP501 |
F | LEU23 |
F | SER436 |
F | GLY439 |
F | TYR440 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue EDO E 503 |
Chain | Residue |
E | ILE29 |
E | LEU431 |
E | ARG435 |
E | HOH603 |
E | HOH606 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue EDO E 504 |
Chain | Residue |
E | ARG16 |
E | PRO17 |
E | ARG452 |
E | GLU454 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue K E 505 |
Chain | Residue |
E | GLU465 |
E | SER466 |
E | HIS467 |
H | GLY296 |
H | GLY298 |
H | CYS301 |
site_id | AE1 |
Number of Residues | 6 |
Details | binding site for residue K F 501 |
Chain | Residue |
E | GLY296 |
E | GLY298 |
E | CYS301 |
F | GLU465 |
F | SER466 |
F | HIS467 |
site_id | AE2 |
Number of Residues | 23 |
Details | binding site for residue IMP F 502 |
Chain | Residue |
F | ALA46 |
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 | 8L1503 |
F | HOH607 |
F | HOH611 |
F | HOH617 |
F | HOH636 |
F | HOH638 |
site_id | AE3 |
Number of Residues | 12 |
Details | binding site for residue 8L1 F 503 |
Chain | Residue |
F | VAL224 |
F | ALA246 |
F | THR303 |
F | MET384 |
F | GLY385 |
F | GLU411 |
F | IMP502 |
G | LEU23 |
G | PRO24 |
G | SER436 |
G | GLY439 |
G | TYR440 |
site_id | AE4 |
Number of Residues | 4 |
Details | binding site for residue EDO F 504 |
Chain | Residue |
F | ASP207 |
F | ARG435 |
F | HOH603 |
F | HOH604 |
site_id | AE5 |
Number of Residues | 6 |
Details | binding site for residue EDO F 505 |
Chain | Residue |
F | ARG16 |
F | PRO17 |
F | GLY18 |
F | ARG452 |
F | ALA453 |
F | GLU454 |
site_id | AE6 |
Number of Residues | 6 |
Details | binding site for residue K G 501 |
Chain | Residue |
F | GLY296 |
F | GLY298 |
F | CYS301 |
G | GLU465 |
G | SER466 |
G | HIS467 |
site_id | AE7 |
Number of Residues | 24 |
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 | MET355 |
G | GLY357 |
G | SER358 |
G | TYR381 |
G | GLY383 |
G | MET384 |
G | GLY385 |
G | GLU411 |
G | GLY412 |
G | 8L1503 |
G | HOH604 |
G | HOH605 |
G | HOH611 |
G | HOH633 |
site_id | AE8 |
Number of Residues | 9 |
Details | binding site for residue 8L1 G 503 |
Chain | Residue |
G | VAL224 |
G | THR303 |
G | MET384 |
G | GLY385 |
G | GLU411 |
G | IMP502 |
H | SER436 |
H | GLY439 |
H | TYR440 |
site_id | AE9 |
Number of Residues | 5 |
Details | binding site for residue IPA G 504 |
Chain | Residue |
G | ILE29 |
G | ASN40 |
G | ASP207 |
G | ARG435 |
G | HOH619 |
site_id | AF1 |
Number of Residues | 6 |
Details | binding site for residue K H 501 |
Chain | Residue |
G | GLY296 |
G | GLY298 |
G | CYS301 |
H | GLU465 |
H | SER466 |
H | HIS467 |
site_id | AF2 |
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 | 8L1503 |
H | HOH612 |
H | HOH624 |
H | HOH625 |
H | HOH627 |
H | HOH641 |
site_id | AF3 |
Number of Residues | 12 |
Details | binding site for residue 8L1 H 503 |
Chain | Residue |
E | SER436 |
E | GLY439 |
E | TYR440 |
H | VAL224 |
H | SER245 |
H | ALA246 |
H | HIS247 |
H | THR303 |
H | GLY385 |
H | GLU411 |
H | IMP502 |
H | HOH677 |
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 |