1LRT
CRYSTAL STRUCTURE OF TERNARY COMPLEX OF TRITRICHOMONAS FOETUS INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE: STRUCTURAL CHARACTERIZATION OF NAD+ SITE IN MICROBIAL ENZYME
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 |
Functional Information from PROSITE/UniProt
| site_id | PS00487 |
| Number of Residues | 13 |
| Details | IMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. IKIGIGgGSICiT |
| Chain | Residue | Details |
| A | ILE309-THR321 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|PubMed:12235158, ECO:0000269|PubMed:12549902 |
| Chain | Residue | Details |
| A | CYS319 | |
| B | CYS319 | |
| C | CYS319 | |
| D | CYS319 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03156 |
| Chain | Residue | Details |
| A | ARG418 | |
| B | ARG418 | |
| C | ARG418 | |
| D | ARG418 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:12549902 |
| Chain | Residue | Details |
| A | GLY20 | |
| B | GLY316 | |
| B | CYS319 | |
| B | ASN460 | |
| C | GLY20 | |
| C | SER22 | |
| C | GLY314 | |
| C | GLY316 | |
| C | CYS319 | |
| C | ASN460 | |
| D | GLY20 | |
| A | SER22 | |
| D | SER22 | |
| D | GLY314 | |
| D | GLY316 | |
| D | CYS319 | |
| D | ASN460 | |
| A | GLY314 | |
| A | GLY316 | |
| A | CYS319 | |
| A | ASN460 | |
| B | GLY20 | |
| B | SER22 | |
| B | GLY314 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 28 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP261 | |
| B | SER317 | |
| B | ASP358 | |
| B | GLY381 | |
| B | TYR405 | |
| B | GLU431 | |
| C | ASP261 | |
| C | GLY312 | |
| C | SER317 | |
| C | ASP358 | |
| C | GLY381 | |
| A | GLY312 | |
| C | TYR405 | |
| C | GLU431 | |
| D | ASP261 | |
| D | GLY312 | |
| D | SER317 | |
| D | ASP358 | |
| D | GLY381 | |
| D | TYR405 | |
| D | GLU431 | |
| A | SER317 | |
| A | ASP358 | |
| A | GLY381 | |
| A | TYR405 | |
| A | GLU431 | |
| B | ASP261 | |
| B | GLY312 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12549902 |
| Chain | Residue | Details |
| A | ASP264 | |
| B | GLY487 | |
| C | ASP264 | |
| C | PHE266 | |
| C | GLU485 | |
| C | GLY486 | |
| C | GLY487 | |
| D | ASP264 | |
| D | PHE266 | |
| D | GLU485 | |
| D | GLY486 | |
| A | PHE266 | |
| D | GLY487 | |
| A | GLU485 | |
| A | GLY486 | |
| A | GLY487 | |
| B | ASP264 | |
| B | PHE266 | |
| B | GLU485 | |
| B | GLY486 |
