1HP1
5'-NUCLEOTIDASE (OPEN FORM) COMPLEX WITH ATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 600 |
| Chain | Residue |
| A | ASP41 |
| A | HIS43 |
| A | ASP84 |
| A | GLN254 |
| A | ZN601 |
| A | CO3602 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 601 |
| Chain | Residue |
| A | HIS252 |
| A | ZN600 |
| A | CO3602 |
| A | ASP84 |
| A | ASN116 |
| A | HIS217 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CO3 A 602 |
| Chain | Residue |
| A | ASP84 |
| A | ASN116 |
| A | HIS117 |
| A | HIS252 |
| A | GLN254 |
| A | THR518 |
| A | GLY519 |
| A | ZN600 |
| A | ZN601 |
| A | HOH949 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 603 |
| Chain | Residue |
| A | TRP47 |
| A | ARG48 |
| A | HOH1196 |
| A | HOH1223 |
| A | HOH1224 |
| A | HOH1381 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 604 |
| Chain | Residue |
| A | ASN342 |
| A | GLN343 |
| A | HOH806 |
| A | HOH854 |
| A | HOH1166 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 605 |
| Chain | Residue |
| A | LYS68 |
| A | GLY148 |
| A | ARG190 |
| A | HOH973 |
| A | HOH1056 |
| A | HOH1089 |
| A | HOH1264 |
| A | HOH1317 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ATP A 606 |
| Chain | Residue |
| A | ARG375 |
| A | ARG379 |
| A | GLY407 |
| A | ARG410 |
| A | PHE429 |
| A | ASN431 |
| A | GLY458 |
| A | PHE498 |
| A | ASP504 |
| A | HOH1133 |
| A | HOH1363 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 17 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
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 | 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 |
