5TH5
Crystal Structure of QueE from Bacillus subtilis with 6-carboxypterin-5'-deoxyadenosyl ester bound
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0008616 | biological_process | queuosine biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016840 | molecular_function | carbon-nitrogen lyase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| A | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0008616 | biological_process | queuosine biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016840 | molecular_function | carbon-nitrogen lyase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0008616 | biological_process | queuosine biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016840 | molecular_function | carbon-nitrogen lyase activity |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0008616 | biological_process | queuosine biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016840 | molecular_function | carbon-nitrogen lyase activity |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| D | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue SF4 A 301 |
| Chain | Residue |
| A | CYS34 |
| A | CYS38 |
| A | CYS41 |
| A | TRP47 |
| A | GLY83 |
| A | GLN110 |
| A | LYS129 |
| A | 7C5302 |
| A | MET303 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | binding site for residue 7C5 A 302 |
| Chain | Residue |
| A | ILE15 |
| A | GLN16 |
| A | GLY17 |
| A | GLU18 |
| A | PHE28 |
| A | ARG30 |
| A | TRP40 |
| A | ASP42 |
| A | SER81 |
| A | GLU108 |
| A | SER127 |
| A | LYS129 |
| A | LYS161 |
| A | VAL163 |
| A | GLN188 |
| A | VAL189 |
| A | ASN191 |
| A | VAL194 |
| A | GLN231 |
| A | HIS233 |
| A | VAL243 |
| A | SF4301 |
| A | MET303 |
| A | HOH407 |
| A | HOH422 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue MET A 303 |
| Chain | Residue |
| A | ASP42 |
| A | SER81 |
| A | GLY82 |
| A | GLY83 |
| A | GLU108 |
| A | THR109 |
| A | GLN110 |
| A | SER127 |
| A | LYS129 |
| A | SF4301 |
| A | 7C5302 |
| A | HOH407 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue SF4 B 301 |
| Chain | Residue |
| B | CYS34 |
| B | CYS38 |
| B | CYS41 |
| B | TRP47 |
| B | GLY83 |
| B | GLN110 |
| B | LYS129 |
| B | 7C5302 |
| B | MET303 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | binding site for residue 7C5 B 302 |
| Chain | Residue |
| B | ILE15 |
| B | GLN16 |
| B | GLY17 |
| B | GLU18 |
| B | PHE28 |
| B | ARG30 |
| B | TRP40 |
| B | ASP42 |
| B | SER81 |
| B | GLU108 |
| B | SER127 |
| B | LYS129 |
| B | LYS161 |
| B | VAL163 |
| B | GLN188 |
| B | VAL189 |
| B | ASN191 |
| B | VAL194 |
| B | GLN231 |
| B | HIS233 |
| B | VAL243 |
| B | SF4301 |
| B | MET303 |
| B | HOH401 |
| B | HOH402 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue MET B 303 |
| Chain | Residue |
| B | ASP42 |
| B | SER81 |
| B | GLY82 |
| B | GLY83 |
| B | GLU108 |
| B | THR109 |
| B | GLN110 |
| B | SER127 |
| B | LYS129 |
| B | SF4301 |
| B | 7C5302 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue SF4 C 301 |
| Chain | Residue |
| C | MET303 |
| C | CYS34 |
| C | CYS38 |
| C | CYS41 |
| C | TRP47 |
| C | GLY83 |
| C | GLN110 |
| C | LYS129 |
| C | 7C5302 |
| site_id | AC8 |
| Number of Residues | 25 |
| Details | binding site for residue 7C5 C 302 |
| Chain | Residue |
| C | ILE15 |
| C | GLN16 |
| C | GLY17 |
| C | GLU18 |
| C | PHE28 |
| C | ARG30 |
| C | TRP40 |
| C | ASP42 |
| C | SER81 |
| C | GLU108 |
| C | SER127 |
| C | LYS129 |
| C | LYS161 |
| C | VAL163 |
| C | GLN188 |
| C | VAL189 |
| C | ASN191 |
| C | VAL194 |
| C | GLN231 |
| C | HIS233 |
| C | VAL243 |
| C | SF4301 |
| C | MET303 |
| C | HOH408 |
| C | HOH446 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | binding site for residue MET C 303 |
| Chain | Residue |
| C | ASP42 |
| C | SER81 |
| C | GLY82 |
| C | GLY83 |
| C | GLU108 |
| C | THR109 |
| C | GLN110 |
| C | SER127 |
| C | LYS129 |
| C | SF4301 |
| C | 7C5302 |
| C | HOH408 |
| site_id | AD1 |
| Number of Residues | 9 |
| Details | binding site for residue SF4 D 301 |
| Chain | Residue |
| D | CYS34 |
| D | CYS38 |
| D | CYS41 |
| D | TRP47 |
| D | GLY83 |
| D | GLN110 |
| D | LYS129 |
| D | 7C5302 |
| D | MET303 |
| site_id | AD2 |
| Number of Residues | 24 |
| Details | binding site for residue 7C5 D 302 |
| Chain | Residue |
| D | ILE15 |
| D | GLN16 |
| D | GLY17 |
| D | GLU18 |
| D | PHE28 |
| D | ARG30 |
| D | TRP40 |
| D | ASP42 |
| D | SER81 |
| D | GLU108 |
| D | SER127 |
| D | LYS129 |
| D | LYS161 |
| D | VAL163 |
| D | GLN188 |
| D | VAL189 |
| D | ASN191 |
| D | VAL194 |
| D | GLN231 |
| D | HIS233 |
| D | VAL243 |
| D | SF4301 |
| D | MET303 |
| D | HOH401 |
| site_id | AD3 |
| Number of Residues | 12 |
| Details | binding site for residue MET D 303 |
| Chain | Residue |
| D | ASP42 |
| D | SER81 |
| D | GLY82 |
| D | GLY83 |
| D | GLU108 |
| D | THR109 |
| D | GLN110 |
| D | SER127 |
| D | LYS129 |
| D | SF4301 |
| D | 7C5302 |
| D | HOH401 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00917 |
| Chain | Residue | Details |
| A | ILE15 | |
| B | ILE15 | |
| B | ARG30 | |
| B | CYS34 | |
| B | CYS38 | |
| B | CYS41 | |
| B | SER43 | |
| B | SER81 | |
| B | GLY83 | |
| B | SER127 | |
| C | ILE15 | |
| A | ARG30 | |
| C | ARG30 | |
| C | CYS34 | |
| C | CYS38 | |
| C | CYS41 | |
| C | SER43 | |
| C | SER81 | |
| C | GLY83 | |
| C | SER127 | |
| D | ILE15 | |
| D | ARG30 | |
| A | CYS34 | |
| D | CYS34 | |
| D | CYS38 | |
| D | CYS41 | |
| D | SER43 | |
| D | SER81 | |
| D | GLY83 | |
| D | SER127 | |
| A | CYS38 | |
| A | CYS41 | |
| A | SER43 | |
| A | SER81 | |
| A | GLY83 | |
| A | SER127 |
