4NJG
Crystal Structure of QueE from Burkholderia multivorans in complex with AdoMet and 6-carboxypterin
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 | 0042802 | molecular_function | identical protein binding |
| 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 | 0042802 | molecular_function | identical protein binding |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 A 301 |
| Chain | Residue |
| A | CYS31 |
| A | TRP34 |
| A | CYS46 |
| A | CYS49 |
| A | GLY92 |
| A | ASN118 |
| A | SAM302 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE SAM A 302 |
| Chain | Residue |
| A | CYS49 |
| A | ASP50 |
| A | THR51 |
| A | THR90 |
| A | GLY91 |
| A | GLY92 |
| A | GLU93 |
| A | GLU116 |
| A | THR117 |
| A | ASN118 |
| A | SER133 |
| A | LYS135 |
| A | LYS149 |
| A | VAL151 |
| A | GLN173 |
| A | PRO174 |
| A | MET175 |
| A | ASP176 |
| A | GLN202 |
| A | SF4301 |
| A | HHS303 |
| A | HOH443 |
| A | GLU15 |
| A | PHE48 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE HHS A 303 |
| Chain | Residue |
| A | LEU12 |
| A | GLY14 |
| A | PHE25 |
| A | ARG27 |
| A | THR90 |
| A | HIS204 |
| A | PRO210 |
| A | SAM302 |
| A | HOH402 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 B 301 |
| Chain | Residue |
| B | CYS31 |
| B | TRP34 |
| B | CYS46 |
| B | CYS49 |
| B | GLY92 |
| B | ASN118 |
| B | SAM302 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE SAM B 302 |
| Chain | Residue |
| B | GLU15 |
| B | PHE48 |
| B | CYS49 |
| B | ASP50 |
| B | THR51 |
| B | THR90 |
| B | GLY91 |
| B | GLY92 |
| B | GLU93 |
| B | GLU116 |
| B | THR117 |
| B | ASN118 |
| B | SER133 |
| B | LYS135 |
| B | LYS149 |
| B | VAL151 |
| B | GLN173 |
| B | PRO174 |
| B | MET175 |
| B | ASP176 |
| B | GLN202 |
| B | SF4301 |
| B | HHS303 |
| B | HOH435 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE HHS B 303 |
| Chain | Residue |
| B | LEU12 |
| B | GLY14 |
| B | PHE25 |
| B | ARG27 |
| B | THR90 |
| B | GLU116 |
| B | HIS204 |
| B | PRO210 |
| B | SAM302 |
| B | HOH446 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24362703 |
| Chain | Residue | Details |
| A | SER133 | |
| A | GLN173 | |
| A | PRO210 | |
| B | LEU12 | |
| B | ARG27 | |
| B | PHE48 | |
| B | THR51 | |
| B | THR90 | |
| B | GLY92 | |
| B | SER133 | |
| B | GLN173 | |
| B | PRO210 | |
| A | LEU12 | |
| A | ARG27 | |
| A | PHE48 | |
| A | THR51 | |
| A | THR90 | |
| A | GLY92 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:24362703 |
| Chain | Residue | Details |
| A | CYS49 | |
| B | CYS31 | |
| B | CYS46 | |
| B | CYS49 | |
| A | CYS31 | |
| A | CYS46 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 943 |
| Chain | Residue | Details |
| A | PHE25 | electrostatic stabiliser |
| A | CYS31 | metal ligand |
| A | CYS46 | metal ligand |
| A | CYS49 | metal ligand |
| A | ASP50 | activator |
| A | THR51 | metal ligand |
| A | GLU116 | proton acceptor, proton donor |
| A | HIS204 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 943 |
| Chain | Residue | Details |
| B | PHE25 | electrostatic stabiliser |
| B | CYS31 | metal ligand |
| B | CYS46 | metal ligand |
| B | CYS49 | metal ligand |
| B | ASP50 | activator |
| B | THR51 | metal ligand |
| B | GLU116 | proton acceptor, proton donor |
| B | HIS204 | electrostatic stabiliser |
