1HO5
5'-NUCLEOTIDASE (E. COLI) IN COMPLEX WITH ADENOSINE AND PHOSPHATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008252 | molecular_function | nucleotidase activity |
| A | 0008253 | molecular_function | 5'-nucleotidase activity |
| A | 0008768 | molecular_function | UDP-sugar diphosphatase activity |
| A | 0009166 | biological_process | nucleotide catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0106411 | molecular_function | XMP 5'-nucleosidase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008252 | molecular_function | nucleotidase activity |
| B | 0008253 | molecular_function | 5'-nucleotidase activity |
| B | 0008768 | molecular_function | UDP-sugar diphosphatase activity |
| B | 0009166 | biological_process | nucleotide catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0106411 | molecular_function | XMP 5'-nucleosidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN A 1601 |
| Chain | Residue |
| A | ASP41 |
| A | HIS43 |
| A | ASP84 |
| A | GLN254 |
| A | MN1602 |
| A | HOH1775 |
| A | HOH1823 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN A 1602 |
| Chain | Residue |
| A | HIS217 |
| A | HIS252 |
| A | MN1601 |
| A | PO41603 |
| A | HOH1823 |
| A | ASP84 |
| A | ASN116 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1603 |
| Chain | Residue |
| A | ASP84 |
| A | ASN116 |
| A | HIS117 |
| A | HIS252 |
| A | ARG375 |
| A | MN1602 |
| A | ADN1604 |
| A | HOH1741 |
| A | HOH1775 |
| A | HOH1823 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 2601 |
| Chain | Residue |
| B | ASP41 |
| B | HIS43 |
| B | ASP84 |
| B | GLN254 |
| B | MN2602 |
| B | HOH2704 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN B 2602 |
| Chain | Residue |
| B | ASP84 |
| B | ASN116 |
| B | HIS217 |
| B | HIS252 |
| B | MN2601 |
| B | PO42603 |
| B | HOH2704 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 2603 |
| Chain | Residue |
| B | ASP84 |
| B | ASN116 |
| B | HIS117 |
| B | ILE178 |
| B | HIS252 |
| B | MN2602 |
| B | ADN2604 |
| B | HOH2704 |
| B | HOH2718 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADN A 1604 |
| Chain | Residue |
| A | ILE178 |
| A | SER405 |
| A | GLY407 |
| A | PHE429 |
| A | ASN431 |
| A | GLY458 |
| A | PHE498 |
| A | ASP504 |
| A | PO41603 |
| A | HOH1756 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADN B 2604 |
| Chain | Residue |
| B | ILE178 |
| B | ASN180 |
| B | SER405 |
| B | GLY407 |
| B | ARG410 |
| B | PHE429 |
| B | ASN431 |
| B | GLY458 |
| B | PHE498 |
| B | ASP504 |
| B | PO42603 |
| B | HOH2718 |
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 | 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 |
