2USH
5'-NUCLEOTIDASE FROM E. COLI
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0009166 | biological_process | nucleotide catabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
A | 0046872 | molecular_function | metal ion binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0009166 | biological_process | nucleotide catabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 601 |
Chain | Residue |
A | ASP41 |
A | HIS43 |
A | ASP84 |
A | GLN254 |
A | ZN602 |
A | HOH883 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 602 |
Chain | Residue |
A | ASP84 |
A | ASN116 |
A | HIS217 |
A | HIS252 |
A | ZN601 |
A | HOH883 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 601 |
Chain | Residue |
B | ASP41 |
B | HIS43 |
B | ASP84 |
B | GLN254 |
B | ZN602 |
B | HOH880 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN B 602 |
Chain | Residue |
B | ASP41 |
B | ASP84 |
B | ASN116 |
B | HIS217 |
B | HIS252 |
B | ZN601 |
B | HOH880 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE WO4 B 701 |
Chain | Residue |
A | WO4702 |
B | LYS322 |
B | WO4704 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE WO4 A 702 |
Chain | Residue |
A | ARG375 |
A | WO4703 |
B | ARG410 |
B | WO4701 |
B | WO4704 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE WO4 A 703 |
Chain | Residue |
A | ARG375 |
A | ARG379 |
A | ARG410 |
A | WO4702 |
A | ZN709 |
B | ARG375 |
B | WO4704 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE WO4 B 704 |
Chain | Residue |
A | WO4702 |
A | WO4703 |
B | ARG410 |
B | WO4701 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN B 705 |
Chain | Residue |
A | ASP194 |
B | HIS226 |
B | GLU235 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN B 706 |
Chain | Residue |
A | HIS226 |
A | GLU235 |
B | GLU225 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 707 |
Chain | Residue |
A | ASP374 |
A | ASP376 |
B | ASP29 |
B | ASP376 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 708 |
Chain | Residue |
A | HIS289 |
A | GLU290 |
A | LYS293 |
B | GLU326 |
site_id | BC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ZN A 709 |
Chain | Residue |
A | WO4703 |
site_id | ZNA |
Number of Residues | 7 |
Details | ZN BINDING SITE |
Chain | Residue |
A | ASP41 |
A | HIS43 |
A | ASP84 |
A | ASN116 |
A | HIS217 |
A | HIS252 |
A | GLN254 |
site_id | ZNB |
Number of Residues | 7 |
Details | ZN BINDING SITE |
Chain | Residue |
B | ASP84 |
B | ASN116 |
B | HIS217 |
B | HIS252 |
B | GLN254 |
B | ASP41 |
B | HIS43 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 18 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP41 | |
B | ASP41 | |
B | HIS43 | |
B | ASP84 | |
B | ASN116 | |
B | HIS217 | |
B | HIS252 | |
B | GLN254 | |
B | ARG375 | |
B | PHE498 | |
A | HIS43 | |
A | ASP84 | |
A | ASN116 | |
A | HIS217 | |
A | HIS252 | |
A | GLN254 | |
A | ARG375 | |
A | PHE498 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | HIS117 | |
A | ASP120 | |
B | HIS117 | |
B | ASP120 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1ush |
Chain | Residue | Details |
A | ARG375 | |
A | ARG410 | |
A | ASP120 | |
A | HIS117 | |
A | ARG379 | |
A | ASN116 |
site_id | CSA2 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1ush |
Chain | Residue | Details |
B | ARG375 | |
B | ARG410 | |
B | ASP120 | |
B | HIS117 | |
B | ARG379 | |
B | ASN116 |
site_id | MCSA1 |
Number of Residues | 12 |
Details | M-CSA 611 |
Chain | Residue | Details |
A | ASP41 | metal ligand |
A | ARG375 | electrostatic stabiliser, increase acidity, increase electrophilicity |
A | ARG379 | electrostatic stabiliser, increase acidity, increase electrophilicity |
A | ARG410 | electrostatic stabiliser, increase acidity, increase electrophilicity |
A | HIS43 | metal ligand |
A | ASP84 | metal ligand |
A | ASN116 | electrostatic stabiliser, metal ligand |
A | HIS117 | electrostatic stabiliser, increase nucleophilicity, metal ligand, proton acceptor |
A | ASP120 | electrostatic stabiliser, increase basicity |
A | HIS217 | metal ligand |
A | HIS252 | metal ligand |
A | GLN254 | metal ligand |
site_id | MCSA2 |
Number of Residues | 12 |
Details | M-CSA 611 |
Chain | Residue | Details |
B | ASP41 | metal ligand |
B | ARG375 | electrostatic stabiliser, increase acidity, increase electrophilicity |
B | ARG379 | electrostatic stabiliser, increase acidity, increase electrophilicity |
B | ARG410 | electrostatic stabiliser, increase acidity, increase electrophilicity |
B | HIS43 | metal ligand |
B | ASP84 | metal ligand |
B | ASN116 | electrostatic stabiliser, metal ligand |
B | HIS117 | electrostatic stabiliser, increase nucleophilicity, metal ligand, proton acceptor |
B | ASP120 | electrostatic stabiliser, increase basicity |
B | HIS217 | metal ligand |
B | HIS252 | metal ligand |
B | GLN254 | metal ligand |