2MAS
PURINE NUCLEOSIDE HYDROLASE WITH A TRANSITION STATE INHIBITOR
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 |
C | 0005829 | cellular_component | cytosol |
C | 0006139 | biological_process | nucleobase-containing compound metabolic process |
C | 0006152 | biological_process | purine nucleoside catabolic process |
C | 0008477 | molecular_function | purine nucleosidase activity |
C | 0009117 | biological_process | nucleotide metabolic process |
C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
C | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
C | 0045437 | molecular_function | uridine nucleosidase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0047724 | molecular_function | inosine nucleosidase activity |
D | 0005829 | cellular_component | cytosol |
D | 0006139 | biological_process | nucleobase-containing compound metabolic process |
D | 0006152 | biological_process | purine nucleoside catabolic process |
D | 0008477 | molecular_function | purine nucleosidase activity |
D | 0009117 | biological_process | nucleotide metabolic process |
D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
D | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
D | 0045437 | molecular_function | uridine nucleosidase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0047724 | molecular_function | inosine nucleosidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 316 |
Chain | Residue |
A | ASP10 |
A | ASP15 |
A | ASN39 |
A | THR126 |
A | ASP242 |
A | PIR400 |
A | HOH436 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA B 316 |
Chain | Residue |
B | ASP10 |
B | ASP15 |
B | ASN39 |
B | THR126 |
B | ASP242 |
B | PIR400 |
B | HOH428 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA C 316 |
Chain | Residue |
C | ASP10 |
C | ASP15 |
C | ASN39 |
C | THR126 |
C | ASP242 |
C | PIR400 |
C | HOH451 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA D 316 |
Chain | Residue |
D | ASP10 |
D | ASP15 |
D | ASN39 |
D | THR126 |
D | ASP242 |
D | PIR400 |
D | HOH441 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PIR A 400 |
Chain | Residue |
A | ASP14 |
A | ASP15 |
A | ASN39 |
A | ILE81 |
A | HIS82 |
A | THR126 |
A | MET152 |
A | ASN160 |
A | GLU166 |
A | ASN168 |
A | ARG233 |
A | ASP242 |
A | CA316 |
A | HOH436 |
site_id | AC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PIR B 400 |
Chain | Residue |
B | ASP14 |
B | ASP15 |
B | ASN39 |
B | ILE81 |
B | HIS82 |
B | THR126 |
B | MET152 |
B | ASN160 |
B | GLU166 |
B | ASN168 |
B | ARG233 |
B | ASP242 |
B | CA316 |
B | HOH428 |
site_id | AC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PIR C 400 |
Chain | Residue |
C | ASP14 |
C | ASP15 |
C | ASN39 |
C | ILE81 |
C | HIS82 |
C | THR126 |
C | MET152 |
C | ASN160 |
C | GLU166 |
C | ASN168 |
C | ASP242 |
C | CA316 |
C | HOH451 |
site_id | AC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PIR D 400 |
Chain | Residue |
D | ASP242 |
D | CA316 |
D | ASP14 |
D | ASP15 |
D | ASN39 |
D | ILE81 |
D | THR126 |
D | MET152 |
D | ASN160 |
D | GLU166 |
D | ASN168 |
D | ARG233 |
site_id | S1 |
Number of Residues | 5 |
Details | DESCRIPTION NOT PROVIDED |
Chain | Residue |
A | ASP10 |
A | ASP15 |
A | ASP242 |
A | HIS241 |
A | HIS82 |
site_id | S2 |
Number of Residues | 5 |
Details | DESCRIPTION NOT PROVIDED |
Chain | Residue |
B | HIS82 |
B | ASP10 |
B | ASP15 |
B | ASP242 |
B | HIS241 |
site_id | S3 |
Number of Residues | 5 |
Details | DESCRIPTION NOT PROVIDED |
Chain | Residue |
C | ASP10 |
C | ASP15 |
C | ASP242 |
C | HIS241 |
C | HIS82 |
site_id | S4 |
Number of Residues | 5 |
Details | DESCRIPTION NOT PROVIDED |
Chain | Residue |
D | ASP10 |
D | ASP15 |
D | ASP242 |
D | HIS241 |
D | HIS82 |
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 | 4 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:8634238 |
Chain | Residue | Details |
A | ASP242 | |
B | ASP242 | |
C | ASP242 | |
D | ASP242 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | PRO11 | |
C | ALA16 | |
C | GLY127 | |
C | PRO243 | |
D | PRO11 | |
D | ALA16 | |
D | GLY127 | |
D | PRO243 | |
A | ALA16 | |
A | GLY127 | |
A | PRO243 | |
B | PRO11 | |
B | ALA16 | |
B | GLY127 | |
B | PRO243 | |
C | PRO11 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8634238 |
Chain | Residue | Details |
A | ASP15 | |
C | ALA161 | |
C | PHE167 | |
C | ILE169 | |
D | ASP15 | |
D | ALA161 | |
D | PHE167 | |
D | ILE169 | |
A | ALA161 | |
A | PHE167 | |
A | ILE169 | |
B | ASP15 | |
B | ALA161 | |
B | PHE167 | |
B | ILE169 | |
C | ASP15 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1mas |
Chain | Residue | Details |
A | ASP10 | |
A | HIS241 | |
A | ASN168 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1mas |
Chain | Residue | Details |
B | ASP10 | |
B | HIS241 | |
B | ASN168 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1mas |
Chain | Residue | Details |
C | ASP10 | |
C | HIS241 | |
C | ASN168 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1mas |
Chain | Residue | Details |
D | ASP10 | |
D | HIS241 | |
D | ASN168 |
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 |
site_id | MCSA3 |
Number of Residues | 8 |
Details | M-CSA 39 |
Chain | Residue | Details |
C | PRO11 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
C | ALA16 | metal ligand |
C | GLN40 | metal ligand |
C | GLY127 | metal ligand |
C | ASN168 | electrostatic stabiliser |
C | ILE169 | electrostatic stabiliser, hydrogen bond donor |
C | ASP242 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
C | PRO243 | metal ligand |
site_id | MCSA4 |
Number of Residues | 8 |
Details | M-CSA 39 |
Chain | Residue | Details |
D | PRO11 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
D | ALA16 | metal ligand |
D | GLN40 | metal ligand |
D | GLY127 | metal ligand |
D | ASN168 | electrostatic stabiliser |
D | ILE169 | electrostatic stabiliser, hydrogen bond donor |
D | ASP242 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | PRO243 | metal ligand |