1MAS
PURINE NUCLEOSIDE HYDROLASE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005829 | cellular_component | cytosol |
A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
A | 0006152 | biological_process | purine nucleoside catabolic process |
A | 0008477 | molecular_function | purine nucleosidase activity |
A | 0009117 | biological_process | nucleotide metabolic process |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
A | 0045437 | molecular_function | uridine nucleosidase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0047724 | molecular_function | inosine nucleosidase activity |
B | 0005829 | cellular_component | cytosol |
B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
B | 0006152 | biological_process | purine nucleoside catabolic process |
B | 0008477 | molecular_function | purine nucleosidase activity |
B | 0009117 | biological_process | nucleotide metabolic process |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
B | 0045437 | molecular_function | uridine nucleosidase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0047724 | molecular_function | inosine nucleosidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K A 900 |
Chain | Residue |
A | ASP10 |
A | ASP15 |
A | THR126 |
A | ASP242 |
A | HOH902 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K B 933 |
Chain | Residue |
B | ASP10 |
B | ASP15 |
B | THR126 |
B | ASP242 |
site_id | ACT |
Number of Residues | 10 |
Details | POCKET AT THE C-TERMINAL END OF THE BETA SHEET. |
Chain | Residue |
A | ASP10 |
B | ASP242 |
A | ASP14 |
A | ASP15 |
A | HIS241 |
A | ASP242 |
B | ASP10 |
B | ASP14 |
B | ASP15 |
B | HIS241 |
Functional Information from PROSITE/UniProt
site_id | PS01247 |
Number of Residues | 11 |
Details | IUNH Inosine-uridine preferring nucleoside hydrolase family signature. DcDPGlDDAVA |
Chain | Residue | Details |
A | ASP8-ALA18 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:8634238 |
Chain | Residue | Details |
A | ASP242 | |
B | ASP242 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
A | PRO11 | |
A | ALA16 | |
A | GLY127 | |
A | PRO243 | |
B | PRO11 | |
B | ALA16 | |
B | GLY127 | |
B | PRO243 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8634238 |
Chain | Residue | Details |
A | ASP15 | |
A | ALA161 | |
A | PHE167 | |
A | ILE169 | |
B | ASP15 | |
B | ALA161 | |
B | PHE167 | |
B | ILE169 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 39 |
Chain | Residue | Details |
A | PRO11 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
A | ALA16 | metal ligand |
A | GLN40 | metal ligand |
A | GLY127 | metal ligand |
A | ASN168 | electrostatic stabiliser |
A | ILE169 | electrostatic stabiliser, hydrogen bond donor |
A | ASP242 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | PRO243 | metal ligand |
site_id | MCSA2 |
Number of Residues | 8 |
Details | M-CSA 39 |
Chain | Residue | Details |
B | PRO11 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
B | ALA16 | metal ligand |
B | GLN40 | metal ligand |
B | GLY127 | metal ligand |
B | ASN168 | electrostatic stabiliser |
B | ILE169 | electrostatic stabiliser, hydrogen bond donor |
B | ASP242 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | PRO243 | metal ligand |