5AXC
Crystal structure of mouse SAHH complexed with 3'-keto aristeromycin
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 | 33 |
Details | binding site for residue NAD A 501 |
Chain | Residue |
A | THR157 |
A | GLU243 |
A | ILE244 |
A | ASP245 |
A | ASN248 |
A | THR275 |
A | THR276 |
A | GLY277 |
A | ILE281 |
A | ILE299 |
A | GLY300 |
A | THR158 |
A | HIS301 |
A | LEU344 |
A | ASN346 |
A | HIS353 |
A | GLN413 |
A | LYS426 |
A | TYR430 |
A | ARJ503 |
A | HOH752 |
A | HOH780 |
A | THR159 |
A | HOH826 |
A | HOH846 |
A | HOH862 |
A | HOH863 |
A | ASN191 |
A | GLY220 |
A | GLY222 |
A | ASP223 |
A | VAL224 |
A | THR242 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue NA A 502 |
Chain | Residue |
A | GLU59 |
A | HOH676 |
A | HOH737 |
A | HOH993 |
C | ASP208 |
C | HOH684 |
site_id | AC3 |
Number of Residues | 15 |
Details | binding site for residue ARJ A 503 |
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 | PHE362 |
A | NAD501 |
site_id | AC4 |
Number of Residues | 32 |
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 | CYS278 |
C | ILE281 |
C | ILE299 |
C | GLY300 |
C | HIS301 |
C | LEU344 |
C | ASN346 |
C | HIS353 |
C | GLN413 |
C | LYS426 |
C | TYR430 |
C | ARJ503 |
C | HOH683 |
C | HOH814 |
C | HOH834 |
C | HOH845 |
C | HOH858 |
C | HOH869 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue NA C 502 |
Chain | Residue |
A | ASP208 |
A | HOH640 |
A | HOH1014 |
C | GLU59 |
C | HOH756 |
C | HOH826 |
site_id | AC6 |
Number of Residues | 16 |
Details | binding site for residue ARJ C 503 |
Chain | Residue |
C | LYS186 |
C | ASP190 |
C | HIS301 |
C | MET351 |
C | HIS353 |
C | MET358 |
C | PHE362 |
C | NAD501 |
C | HOH602 |
C | HIS55 |
C | THR57 |
C | GLU59 |
C | THR60 |
C | ASP131 |
C | GLU156 |
C | THR157 |
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 |