1HP1
5'-NUCLEOTIDASE (OPEN FORM) COMPLEX WITH ATP
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 |
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 | 9 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP41 | |
A | HIS43 | |
A | ASP84 | |
A | ASN116 | |
A | HIS217 | |
A | HIS252 | |
A | GLN254 | |
A | ASN384 | |
A | PRO507 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | HIS117 | |
A | 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 | MCSA1 |
Number of Residues | 12 |
Details | M-CSA 611 |
Chain | Residue | Details |
A | ASP41 | metal ligand |
A | ASN384 | electrostatic stabiliser, increase acidity, increase electrophilicity |
A | LEU388 | electrostatic stabiliser, increase acidity, increase electrophilicity |
A | SER419 | 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 |