6XI9
X-ray crystal structure of MqnE from Pedobacter heparinus in complex with aminofutalosine and methionine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0009234 | biological_process | menaquinone biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
A | 0044689 | molecular_function | 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase 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 | 0102573 | molecular_function | aminodeoxyfutalosine synthase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0009234 | biological_process | menaquinone biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
B | 0044689 | molecular_function | 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase 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 | 0102573 | molecular_function | aminodeoxyfutalosine synthase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue SF4 A 401 |
Chain | Residue |
A | CYS80 |
A | CYS84 |
A | CYS87 |
A | LYS207 |
A | MET402 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue MET A 402 |
Chain | Residue |
A | GLY190 |
A | GLY191 |
A | LYS207 |
A | SF4401 |
A | V47403 |
A | THR125 |
A | GLY126 |
A | THR157 |
A | VAL159 |
site_id | AC3 |
Number of Residues | 20 |
Details | binding site for residue V47 A 403 |
Chain | Residue |
A | PHE86 |
A | LYS154 |
A | PRO188 |
A | GLY189 |
A | GLY190 |
A | GLY191 |
A | GLU193 |
A | ASN228 |
A | THR230 |
A | LEU232 |
A | ILE263 |
A | LYS266 |
A | ARG268 |
A | ASN272 |
A | LYS303 |
A | ASP326 |
A | MET402 |
A | CL404 |
A | HOH632 |
A | HOH677 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue CL A 404 |
Chain | Residue |
A | HIS123 |
A | THR125 |
A | THR157 |
A | PRO188 |
A | GLY190 |
A | V47403 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue SF4 B 401 |
Chain | Residue |
B | CYS80 |
B | CYS84 |
B | CYS87 |
B | LYS207 |
B | MET402 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue MET B 402 |
Chain | Residue |
B | GLY126 |
B | THR157 |
B | VAL159 |
B | GLY191 |
B | LYS207 |
B | SF4401 |
B | V47403 |
site_id | AC7 |
Number of Residues | 19 |
Details | binding site for residue V47 B 403 |
Chain | Residue |
B | PHE86 |
B | PRO188 |
B | GLY189 |
B | GLY190 |
B | GLY191 |
B | GLU193 |
B | ASN228 |
B | THR230 |
B | LEU232 |
B | ILE263 |
B | LEU265 |
B | LYS266 |
B | PHE267 |
B | ARG268 |
B | TYR305 |
B | MET402 |
B | HOH502 |
B | HOH568 |
B | HOH597 |