5UUZ
Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with IMP and the 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 | 21 |
Details | binding site for residue IMP A 501 |
Chain | Residue |
A | ALA49 |
A | GLY343 |
A | MET362 |
A | GLY364 |
A | SER365 |
A | TYR388 |
A | GLY390 |
A | MET391 |
A | GLY392 |
A | GLU416 |
A | GLY417 |
A | MET51 |
A | 8L4502 |
A | HOH612 |
A | ASN280 |
A | GLY305 |
A | SER306 |
A | ILE307 |
A | CYS308 |
A | ASP341 |
A | GLY342 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue 8L4 A 502 |
Chain | Residue |
A | ALA253 |
A | THR310 |
A | MET391 |
A | GLY392 |
A | VAL414 |
A | GLU416 |
A | IMP501 |
A | HOH602 |
C | PRO27 |
C | ALA441 |
C | GLY444 |
C | TYR445 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue K A 503 |
Chain | Residue |
A | GLU470 |
A | SER471 |
A | HIS472 |
B | GLY303 |
B | GLY305 |
B | CYS308 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue K A 504 |
Chain | Residue |
A | GLY303 |
A | GLY305 |
A | CYS308 |
C | GLU470 |
C | SER471 |
C | HIS472 |
site_id | AC5 |
Number of Residues | 19 |
Details | binding site for residue IMP B 500 |
Chain | Residue |
B | ALA49 |
B | MET51 |
B | GLY305 |
B | SER306 |
B | ILE307 |
B | CYS308 |
B | ASP341 |
B | GLY342 |
B | GLY343 |
B | MET362 |
B | GLY364 |
B | SER365 |
B | TYR388 |
B | GLY390 |
B | MET391 |
B | GLY392 |
B | GLU416 |
B | GLY417 |
B | 8L4501 |
site_id | AC6 |
Number of Residues | 11 |
Details | binding site for residue 8L4 B 501 |
Chain | Residue |
A | PRO27 |
A | ALA441 |
A | GLY444 |
A | TYR445 |
B | ALA253 |
B | THR310 |
B | MET391 |
B | GLY392 |
B | VAL414 |
B | GLU416 |
B | IMP500 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue K B 502 |
Chain | Residue |
B | GLU470 |
B | SER471 |
B | HIS472 |
D | GLY303 |
D | GLY305 |
D | CYS308 |
site_id | AC8 |
Number of Residues | 21 |
Details | binding site for residue IMP C 501 |
Chain | Residue |
C | 8L4502 |
C | HOH616 |
C | HOH619 |
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 | GLY417 |
site_id | AC9 |
Number of Residues | 12 |
Details | binding site for residue 8L4 C 502 |
Chain | Residue |
C | ALA253 |
C | THR310 |
C | MET391 |
C | GLY392 |
C | VAL414 |
C | GLU416 |
C | IMP501 |
C | HOH601 |
D | PRO27 |
D | ALA441 |
D | GLY444 |
D | TYR445 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue K C 503 |
Chain | Residue |
C | GLY303 |
C | GLY305 |
C | CYS308 |
D | GLU470 |
D | SER471 |
D | HIS472 |
site_id | AD2 |
Number of Residues | 22 |
Details | binding site for residue IMP D 501 |
Chain | Residue |
D | ALA49 |
D | MET51 |
D | ASN280 |
D | GLY305 |
D | SER306 |
D | ILE307 |
D | CYS308 |
D | ASP341 |
D | GLY343 |
D | MET362 |
D | GLY364 |
D | SER365 |
D | TYR388 |
D | GLY390 |
D | MET391 |
D | GLY392 |
D | GLU416 |
D | GLY417 |
D | 8L4502 |
D | HOH608 |
D | HOH618 |
D | HOH619 |
site_id | AD3 |
Number of Residues | 12 |
Details | binding site for residue 8L4 D 502 |
Chain | Residue |
B | PRO27 |
B | ALA441 |
B | GLY444 |
B | TYR445 |
D | ALA253 |
D | HIS254 |
D | THR310 |
D | MET391 |
D | GLY392 |
D | VAL414 |
D | GLU416 |
D | IMP501 |
site_id | AD4 |
Number of Residues | 19 |
Details | binding site for residue IMP E 501 |
Chain | Residue |
E | ALA49 |
E | MET51 |
E | GLY305 |
E | SER306 |
E | ILE307 |
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 | 8L4502 |
site_id | AD5 |
Number of Residues | 11 |
Details | binding site for residue 8L4 E 502 |
Chain | Residue |
E | ALA253 |
E | THR310 |
E | MET391 |
E | GLY392 |
E | VAL414 |
E | GLU416 |
E | IMP501 |
G | PRO27 |
G | ALA441 |
G | GLY444 |
G | TYR445 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue K E 503 |
Chain | Residue |
E | GLU470 |
E | SER471 |
E | HIS472 |
F | GLY303 |
F | GLY305 |
F | CYS308 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue K E 504 |
Chain | Residue |
E | GLY303 |
E | GLY305 |
E | CYS308 |
G | GLU470 |
G | SER471 |
G | HIS472 |
site_id | AD8 |
Number of Residues | 20 |
Details | binding site for residue IMP F 500 |
Chain | Residue |
F | ALA49 |
F | MET51 |
F | ASN280 |
F | GLY305 |
F | SER306 |
F | ILE307 |
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 | 8L4501 |
site_id | AD9 |
Number of Residues | 10 |
Details | binding site for residue 8L4 F 501 |
Chain | Residue |
E | PRO27 |
E | GLY444 |
E | TYR445 |
F | ALA253 |
F | THR310 |
F | MET391 |
F | GLY392 |
F | VAL414 |
F | GLU416 |
F | IMP500 |
site_id | AE1 |
Number of Residues | 6 |
Details | binding site for residue K F 502 |
Chain | Residue |
F | GLU470 |
F | SER471 |
F | HIS472 |
H | GLY303 |
H | GLY305 |
H | CYS308 |
site_id | AE2 |
Number of Residues | 20 |
Details | binding site for residue IMP G 501 |
Chain | Residue |
G | ALA49 |
G | MET51 |
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 | 8L4502 |
G | HOH601 |
G | HOH604 |
site_id | AE3 |
Number of Residues | 11 |
Details | binding site for residue 8L4 G 502 |
Chain | Residue |
G | ALA253 |
G | HIS254 |
G | THR310 |
G | MET391 |
G | GLY392 |
G | GLU416 |
G | IMP501 |
H | PRO27 |
H | ALA441 |
H | GLY444 |
H | TYR445 |
site_id | AE4 |
Number of Residues | 6 |
Details | binding site for residue K G 503 |
Chain | Residue |
G | GLY303 |
G | GLY305 |
G | CYS308 |
H | GLU470 |
H | SER471 |
H | HIS472 |
site_id | AE5 |
Number of Residues | 16 |
Details | binding site for residue IMP H 501 |
Chain | Residue |
H | ALA49 |
H | MET51 |
H | GLY305 |
H | SER306 |
H | ILE307 |
H | CYS308 |
H | ASP341 |
H | GLY343 |
H | GLY364 |
H | SER365 |
H | TYR388 |
H | GLY390 |
H | MET391 |
H | GLY392 |
H | GLU416 |
H | 8L4502 |
site_id | AE6 |
Number of Residues | 13 |
Details | binding site for residue 8L4 H 502 |
Chain | Residue |
F | ALA441 |
F | GLY444 |
F | TYR445 |
H | THR252 |
H | ALA253 |
H | HIS254 |
H | THR310 |
H | MET391 |
H | GLY392 |
H | MET397 |
H | VAL414 |
H | GLU416 |
H | IMP501 |
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 |