5AXD
Crystal structure of mouse SAHH complexed with ribavirin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002439 | biological_process | chronic inflammatory response to antigenic stimulus |
| A | 0004013 | molecular_function | adenosylhomocysteinase activity |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005829 | cellular_component | cytosol |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0007584 | biological_process | response to nutrient |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019510 | biological_process | S-adenosylhomocysteine catabolic process |
| A | 0030554 | molecular_function | adenyl nucleotide binding |
| A | 0033353 | biological_process | S-adenosylmethionine cycle |
| A | 0042470 | cellular_component | melanosome |
| A | 0042745 | biological_process | circadian sleep/wake cycle |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0051287 | molecular_function | NAD binding |
| C | 0002439 | biological_process | chronic inflammatory response to antigenic stimulus |
| C | 0004013 | molecular_function | adenosylhomocysteinase activity |
| C | 0005507 | molecular_function | copper ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| C | 0005829 | cellular_component | cytosol |
| C | 0006730 | biological_process | one-carbon metabolic process |
| C | 0007584 | biological_process | response to nutrient |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0019510 | biological_process | S-adenosylhomocysteine catabolic process |
| C | 0030554 | molecular_function | adenyl nucleotide binding |
| C | 0033353 | biological_process | S-adenosylmethionine cycle |
| C | 0042470 | cellular_component | melanosome |
| C | 0042745 | biological_process | circadian sleep/wake cycle |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | binding site for residue NAD A 501 |
| Chain | Residue |
| A | THR157 |
| A | ILE244 |
| A | ASP245 |
| A | ASN248 |
| A | THR275 |
| A | THR276 |
| A | GLY277 |
| A | CYS278 |
| A | ILE281 |
| A | ILE299 |
| A | GLY300 |
| A | THR158 |
| A | HIS301 |
| A | ASN346 |
| A | HIS353 |
| A | GLN413 |
| A | LYS426 |
| A | TYR430 |
| A | RBV502 |
| A | HOH609 |
| A | HOH676 |
| A | HOH710 |
| A | THR159 |
| A | HOH731 |
| A | HOH855 |
| A | HOH868 |
| A | HOH871 |
| A | HOH929 |
| A | ASN191 |
| A | GLY222 |
| A | ASP223 |
| A | VAL224 |
| A | THR242 |
| A | GLU243 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for residue RBV A 502 |
| Chain | Residue |
| A | HIS55 |
| A | THR57 |
| A | GLU59 |
| A | THR60 |
| A | ASP131 |
| A | GLU156 |
| A | THR157 |
| A | LYS186 |
| A | ASP190 |
| A | HIS301 |
| A | MET351 |
| A | HIS353 |
| A | MET358 |
| A | NAD501 |
| A | HOH601 |
| site_id | AC3 |
| Number of Residues | 33 |
| Details | binding site for residue NAD C 501 |
| Chain | Residue |
| C | THR157 |
| C | THR158 |
| C | THR159 |
| C | ASN191 |
| C | GLY222 |
| C | ASP223 |
| C | VAL224 |
| C | THR242 |
| C | GLU243 |
| C | ILE244 |
| C | ASP245 |
| C | ASN248 |
| C | THR275 |
| C | THR276 |
| C | GLY277 |
| C | CYS278 |
| C | ILE281 |
| C | ILE299 |
| C | GLY300 |
| C | HIS301 |
| C | ASN346 |
| C | HIS353 |
| C | GLN413 |
| C | LYS426 |
| C | TYR430 |
| C | RBV502 |
| C | HOH610 |
| C | HOH719 |
| C | HOH747 |
| C | HOH827 |
| C | HOH848 |
| C | HOH879 |
| C | HOH908 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue RBV C 502 |
| Chain | Residue |
| C | HIS55 |
| C | THR57 |
| C | GLU59 |
| C | THR60 |
| C | ASP131 |
| C | GLU156 |
| C | THR157 |
| C | LYS186 |
| C | ASP190 |
| C | HIS301 |
| C | MET351 |
| C | HIS353 |
| C | MET358 |
| C | NAD501 |
| C | HOH601 |
Functional Information from PROSITE/UniProt
| site_id | PS00738 |
| Number of Residues | 15 |
| Details | ADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiFSTQDhAAAAI |
| Chain | Residue | Details |
| A | SER78-ILE92 |
| site_id | PS00739 |
| Number of Residues | 17 |
| Details | ADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKvavVaGYGdVGKGc.A |
| Chain | Residue | Details |
| A | GLY213-ALA229 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P10760 |
| Chain | Residue | Details |
| A | THR57 | |
| C | ASP190 | |
| A | ASP131 | |
| A | GLU156 | |
| A | LYS186 | |
| A | ASP190 | |
| C | THR57 | |
| C | ASP131 | |
| C | GLU156 | |
| C | LYS186 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P23526 |
| Chain | Residue | Details |
| A | SER2 | |
| C | SER2 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P23526 |
| Chain | Residue | Details |
| A | SER183 | |
| C | SER183 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P23526 |
| Chain | Residue | Details |
| A | LYS186 | |
| C | LYS186 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:21183079 |
| Chain | Residue | Details |
| A | TYR193 | |
| C | TYR193 |
