Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008253 | molecular_function | 5'-nucleotidase 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 | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008253 | molecular_function | 5'-nucleotidase 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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN A 1595 |
| Chain | Residue |
| A | ASP44 |
| A | ASP94 |
| A | ASN126 |
| A | HIS227 |
| A | ASP250 |
| A | ZN1596 |
| A | PO41597 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 1596 |
| Chain | Residue |
| A | ASP94 |
| A | HIS252 |
| A | ZN1595 |
| A | PO41597 |
| A | ASP44 |
| A | HIS46 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1597 |
| Chain | Residue |
| A | ASP44 |
| A | ASP94 |
| A | ASN126 |
| A | HIS127 |
| A | LYS187 |
| A | ASP250 |
| A | HIS252 |
| A | ZN1595 |
| A | ZN1596 |
| A | A121598 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE A12 A 1598 |
| Chain | Residue |
| A | HIS127 |
| A | SER191 |
| A | ARG397 |
| A | ASN432 |
| A | GLY434 |
| A | GLY435 |
| A | ARG437 |
| A | PHE456 |
| A | ASN458 |
| A | SER486 |
| A | GLY488 |
| A | TYR540 |
| A | ASP546 |
| A | PO41597 |
| A | HOH2054 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN B 1588 |
| Chain | Residue |
| B | ASP44 |
| B | ASP94 |
| B | ASN126 |
| B | HIS227 |
| B | ASP250 |
| B | ZN1589 |
| B | HOH2007 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 1589 |
| Chain | Residue |
| B | ASP44 |
| B | HIS46 |
| B | ASP94 |
| B | HIS252 |
| B | ZN1588 |
| B | HOH2007 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE A12 B 1590 |
| Chain | Residue |
| B | ASN432 |
| B | GLY434 |
| B | PHE456 |
| B | ASN458 |
| B | SER486 |
| B | GLY488 |
| B | TYR540 |
| B | ASP546 |
| B | HOH2169 |
Functional Information from PROSITE/UniProt
| site_id | PS00785 |
| Number of Residues | 13 |
| Details | 5_NUCLEOTIDASE_1 5'-nucleotidase signature 1. LsILHInDhHSyL |
| Chain | Residue | Details |
| A | LEU37-LEU49 | |
| site_id | PS00786 |
| Number of Residues | 12 |
| Details | 5_NUCLEOTIDASE_2 5'-nucleotidase signature 2. FhyftLGNHEFD |
| Chain | Residue | Details |
| A | PHE119-ASP130 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | HIS227 | |
| A | ARG397 | |
| A | ARG437 | |
| A | PHE456 | |
| B | ASP44 | |
| B | HIS46 | |
| B | ASP94 | |
| B | ASN126 | |
| B | HIS227 | |
| B | ARG397 | |
| B | ARG437 | |
| B | PHE456 | |
| A | ASP44 | |
| A | HIS46 | |
| A | ASP94 | |
| A | ASN126 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR540 | |
| B | TYR540 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | HIS127 | |
| A | ASP130 | |
| B | HIS127 | |
| B | ASP130 | |
