4NJH
Crystal Structure of QueE from Burkholderia multivorans in complex with AdoMet and 6-carboxy-5,6,7,8-tetrahydropterin
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 | 8 |
Details | BINDING SITE FOR RESIDUE SF4 A 301 |
Chain | Residue |
A | CYS31 |
A | TRP34 |
A | CYS46 |
A | CYS49 |
A | GLY92 |
A | ASN118 |
A | LYS135 |
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 | 2K8303 |
A | HOH401 |
A | HOH412 |
A | PHE48 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 2K8 A 303 |
Chain | Residue |
A | THR11 |
A | LEU12 |
A | GLN13 |
A | GLY14 |
A | PHE25 |
A | ARG27 |
A | THR90 |
A | GLU116 |
A | HIS204 |
A | PRO210 |
A | SAM302 |
A | NA304 |
A | HOH484 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NA A 304 |
Chain | Residue |
A | ARG27 |
A | ASP50 |
A | THR51 |
A | 2K8303 |
A | HOH401 |
A | HOH503 |
A | HOH504 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 305 |
Chain | Residue |
A | ARG21 |
A | HIS84 |
A | HOH471 |
A | HOH517 |
A | HOH554 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 B 301 |
Chain | Residue |
B | CYS31 |
B | TRP34 |
B | CYS46 |
B | CYS49 |
B | GLY92 |
B | ASN118 |
B | LYS135 |
B | SAM302 |
site_id | AC7 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE SAM B 302 |
Chain | Residue |
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 | 2K8303 |
B | HOH405 |
B | HOH406 |
site_id | AC8 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 2K8 B 303 |
Chain | Residue |
B | SAM302 |
B | NA304 |
B | HOH484 |
B | THR11 |
B | LEU12 |
B | GLN13 |
B | GLY14 |
B | PHE25 |
B | ARG27 |
B | THR90 |
B | GLU116 |
B | HIS204 |
B | PRO210 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 304 |
Chain | Residue |
B | ARG27 |
B | THR51 |
B | 2K8303 |
B | HOH406 |
B | HOH421 |
B | HOH424 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B 305 |
Chain | Residue |
A | HOH592 |
B | ARG21 |
B | HIS84 |
B | HOH504 |
B | HOH511 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA B 306 |
Chain | Residue |
B | GLN154 |
B | HOH544 |
B | HOH545 |
B | HOH553 |
B | HOH554 |
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 | LEU12 | |
B | LEU12 | |
B | ARG27 | |
B | PHE48 | |
B | THR51 | |
B | THR90 | |
B | GLY92 | |
B | SER133 | |
B | GLN173 | |
B | PRO210 | |
A | ARG27 | |
A | PHE48 | |
A | THR51 | |
A | THR90 | |
A | GLY92 | |
A | SER133 | |
A | GLN173 | |
A | PRO210 |
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 | CYS31 | |
A | CYS46 | |
A | CYS49 | |
B | CYS31 | |
B | CYS46 | |
B | CYS49 |
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 |