6NMM
Ternary complex structure of the T130K mutant of ANT-4 with Neomycin, AMPCPP and Pyrophosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0046677 | biological_process | response to antibiotic |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016779 | molecular_function | nucleotidyltransferase activity |
| C | 0046677 | biological_process | response to antibiotic |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016779 | molecular_function | nucleotidyltransferase activity |
| D | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue PPV A 802 |
| Chain | Residue |
| A | GLY38 |
| A | HOH901 |
| A | HOH904 |
| A | HOH913 |
| A | HOH925 |
| A | HOH930 |
| D | LYS149 |
| A | SER39 |
| A | ARG42 |
| A | SER49 |
| A | ASP50 |
| A | GLU52 |
| A | THR187 |
| A | AMP801 |
| A | MG804 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 803 |
| Chain | Residue |
| A | ASP50 |
| A | GLU52 |
| A | NMY800 |
| A | AMP801 |
| A | HOH901 |
| A | HOH941 |
| D | GLU145 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 804 |
| Chain | Residue |
| A | ASP50 |
| A | GLU52 |
| A | AMP801 |
| A | PPV802 |
| A | HOH901 |
| A | HOH904 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue PPV B 802 |
| Chain | Residue |
| B | SER39 |
| B | ARG42 |
| B | SER49 |
| B | ASP50 |
| B | GLU52 |
| B | THR187 |
| B | AMP801 |
| B | MG804 |
| B | HOH910 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 803 |
| Chain | Residue |
| B | ASP50 |
| B | GLU52 |
| B | NMY800 |
| B | AMP801 |
| B | MG804 |
| C | GLU145 |
| C | HOH923 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 804 |
| Chain | Residue |
| B | ASP50 |
| B | GLU52 |
| B | AMP801 |
| B | PPV802 |
| B | MG803 |
| B | HOH924 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | binding site for residue PPV C 802 |
| Chain | Residue |
| B | LYS149 |
| C | GLY38 |
| C | SER39 |
| C | ARG42 |
| C | SER49 |
| C | ASP50 |
| C | GLU52 |
| C | THR187 |
| C | AMP801 |
| C | MG803 |
| C | HOH902 |
| C | HOH920 |
| C | HOH936 |
| C | HOH958 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 803 |
| Chain | Residue |
| C | ASP50 |
| C | GLU52 |
| C | PPV802 |
| C | HOH902 |
| C | HOH904 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue MG C 804 |
| Chain | Residue |
| B | GLU145 |
| C | ASP50 |
| C | GLU52 |
| C | NMY800 |
| C | AMP801 |
| C | HOH902 |
| C | HOH945 |
| site_id | AD1 |
| Number of Residues | 13 |
| Details | binding site for residue PPV D 802 |
| Chain | Residue |
| A | LYS149 |
| D | GLY38 |
| D | SER39 |
| D | ARG42 |
| D | SER49 |
| D | ASP50 |
| D | GLU52 |
| D | THR187 |
| D | AMP801 |
| D | MG804 |
| D | HOH902 |
| D | HOH913 |
| D | HOH918 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 803 |
| Chain | Residue |
| A | GLU145 |
| D | ASP50 |
| D | GLU52 |
| D | NMY800 |
| D | AMP801 |
| D | HOH907 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 804 |
| Chain | Residue |
| D | HOH902 |
| D | HOH920 |
| D | ASP50 |
| D | GLU52 |
| D | AMP801 |
| D | PPV802 |
| site_id | AD4 |
| Number of Residues | 27 |
| Details | binding site for Di-nucleotide NMY A 800 and A A 801 |
| Chain | Residue |
| A | TYR37 |
| A | GLY38 |
| A | ARG42 |
| A | GLU52 |
| A | GLU63 |
| A | GLU67 |
| A | GLU76 |
| A | ASP80 |
| A | TYR88 |
| A | LEU98 |
| A | THR99 |
| A | GLN102 |
| A | PPV802 |
| A | MG803 |
| A | MG804 |
| A | AMP806 |
| A | HOH901 |
| A | HOH903 |
| A | HOH913 |
| A | HOH918 |
| A | HOH922 |
| A | HOH936 |
| A | HOH947 |
| A | HOH948 |
| D | GLU141 |
| D | GLU145 |
| D | LYS149 |
| site_id | AD5 |
| Number of Residues | 11 |
| Details | binding site for Di-nucleotide NMY A 805 and A A 806 |
| Chain | Residue |
| A | GLU61 |
| A | GLU63 |
| A | PHE64 |
| A | SER65 |
| A | ASN78 |
| A | PHE79 |
| A | ASP80 |
| A | NMY800 |
| A | HOH917 |
| A | HOH922 |
| D | ASP87 |
| site_id | AD6 |
| Number of Residues | 18 |
| Details | binding site for Di-peptide NMY A 805 and ASP C 29 |
| Chain | Residue |
| A | TYR27 |
| A | GLY28 |
| A | ASP30 |
| A | VAL31 |
| A | GLU61 |
| A | GLU63 |
| A | PHE64 |
| A | AMP806 |
| B | ASP87 |
| C | TYR27 |
| C | GLY28 |
| C | ASP30 |
| C | VAL31 |
| C | GLU61 |
| C | GLU63 |
| C | PHE64 |
| C | AMP806 |
| D | ASP87 |
| site_id | AD7 |
| Number of Residues | 24 |
| Details | binding site for Di-nucleotide NMY B 800 and A B 801 |
| Chain | Residue |
| B | TYR37 |
| B | GLY38 |
| B | ARG42 |
| B | GLU52 |
| B | GLU63 |
| B | GLU67 |
| B | GLU76 |
| B | ASP80 |
| B | TYR88 |
| B | LEU98 |
| B | THR99 |
| B | GLN102 |
| B | PPV802 |
| B | MG803 |
| B | MG804 |
| B | HOH901 |
| B | HOH902 |
| B | HOH905 |
| B | HOH912 |
| B | HOH927 |
| B | HOH938 |
| C | GLU141 |
| C | GLU145 |
| C | LYS149 |
| site_id | AD8 |
| Number of Residues | 27 |
| Details | binding site for Di-nucleotide NMY C 800 and A C 801 |
| Chain | Residue |
| B | GLU141 |
| B | GLU145 |
| C | TYR37 |
| C | GLY38 |
| C | ARG42 |
| C | GLU52 |
| C | GLU63 |
| C | GLU67 |
| C | GLU76 |
| C | ASP80 |
| C | TYR88 |
| C | LEU98 |
| C | THR99 |
| C | GLN102 |
| C | PPV802 |
| C | MG804 |
| C | AMP806 |
| C | HOH901 |
| C | HOH902 |
| C | HOH913 |
| C | HOH914 |
| C | HOH921 |
| C | HOH925 |
| C | HOH927 |
| C | HOH936 |
| C | HOH943 |
| C | HOH956 |
| site_id | AD9 |
| Number of Residues | 10 |
| Details | binding site for Di-nucleotide NMY C 805 and A C 806 |
| Chain | Residue |
| B | ASP87 |
| C | GLU61 |
| C | GLU63 |
| C | PHE64 |
| C | SER65 |
| C | ASN78 |
| C | PHE79 |
| C | ASP80 |
| C | NMY800 |
| C | HOH921 |
| site_id | AE1 |
| Number of Residues | 24 |
| Details | binding site for Di-nucleotide NMY D 800 and A D 801 |
| Chain | Residue |
| A | GLU141 |
| A | GLU145 |
| A | LYS149 |
| A | HOH909 |
| D | TYR37 |
| D | GLY38 |
| D | ARG42 |
| D | GLU52 |
| D | GLU63 |
| D | GLU67 |
| D | GLU76 |
| D | ASP80 |
| D | TYR88 |
| D | LEU98 |
| D | THR99 |
| D | GLN102 |
| D | THR186 |
| D | PPV802 |
| D | MG803 |
| D | MG804 |
| D | HOH902 |
| D | HOH908 |
| D | HOH911 |
| D | HOH922 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 452 |
| Details | Region: {"description":"C-terminal domain","evidences":[{"source":"PubMed","id":"7577914","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8218273","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"7577914","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7577914","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1KNY","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"6P06","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"38250052","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NML","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NMM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NMN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21040710","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6UN8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"6UN8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7577914","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KNY","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"38250052","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NMK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NML","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NMN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P01","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P04","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6UN8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7577914","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1KNY","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 647 |
| Chain | Residue | Details |
| A | ASP50 | metal ligand |
| A | GLU52 | metal ligand |
| A | GLU145 | activator, proton acceptor, proton donor |
| A | LYS149 | electrostatic stabiliser, polar interaction |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 647 |
| Chain | Residue | Details |
| B | ASP50 | metal ligand |
| B | GLU52 | metal ligand |
| B | GLU145 | activator, proton acceptor, proton donor |
| B | LYS149 | electrostatic stabiliser, polar interaction |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 647 |
| Chain | Residue | Details |
| C | ASP50 | metal ligand |
| C | GLU52 | metal ligand |
| C | GLU145 | activator, proton acceptor, proton donor |
| C | LYS149 | electrostatic stabiliser, polar interaction |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 647 |
| Chain | Residue | Details |
| D | ASP50 | metal ligand |
| D | GLU52 | metal ligand |
| D | GLU145 | activator, proton acceptor, proton donor |
| D | LYS149 | electrostatic stabiliser, polar interaction |
