3BL5
Crystal structure of QueC from Bacillus subtilis: an enzyme involved in preQ1 biosynthesis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008616 | biological_process | tRNA queuosine(34) biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008616 | biological_process | tRNA queuosine(34) biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0008616 | biological_process | tRNA queuosine(34) biosynthetic process |
| C | 0016874 | molecular_function | ligase activity |
| C | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0008616 | biological_process | tRNA queuosine(34) biosynthetic process |
| D | 0016874 | molecular_function | ligase activity |
| D | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0008270 | molecular_function | zinc ion binding |
| E | 0008616 | biological_process | tRNA queuosine(34) biosynthetic process |
| E | 0016874 | molecular_function | ligase activity |
| E | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0008270 | molecular_function | zinc ion binding |
| F | 0008616 | biological_process | tRNA queuosine(34) biosynthetic process |
| F | 0016874 | molecular_function | ligase activity |
| F | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 300 |
| Chain | Residue |
| A | CYS186 |
| A | TYR187 |
| A | ASN188 |
| A | CYS195 |
| A | CYS198 |
| A | CYS201 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 400 |
| Chain | Residue |
| A | SER11 |
| A | GLY13 |
| A | SER16 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 500 |
| Chain | Residue |
| A | GLY13 |
| A | GLN14 |
| A | ASP15 |
| A | LEU184 |
| A | THR185 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 300 |
| Chain | Residue |
| B | CYS186 |
| B | TYR187 |
| B | ASN188 |
| B | CYS195 |
| B | CYS198 |
| B | CYS201 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 400 |
| Chain | Residue |
| B | SER11 |
| B | GLY13 |
| B | SER16 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 500 |
| Chain | Residue |
| B | GLY13 |
| B | GLN14 |
| B | ASP15 |
| B | LEU184 |
| B | THR185 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 300 |
| Chain | Residue |
| C | CYS186 |
| C | CYS195 |
| C | GLY196 |
| C | CYS198 |
| C | CYS201 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 400 |
| Chain | Residue |
| C | SER11 |
| C | SER16 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 C 500 |
| Chain | Residue |
| C | GLY13 |
| C | GLN14 |
| C | ASP15 |
| C | LEU184 |
| C | THR185 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 300 |
| Chain | Residue |
| D | CYS186 |
| D | CYS195 |
| D | GLY196 |
| D | CYS198 |
| D | CYS201 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG D 400 |
| Chain | Residue |
| D | SER11 |
| D | SER16 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 D 500 |
| Chain | Residue |
| D | GLY13 |
| D | GLN14 |
| D | ASP15 |
| D | LEU184 |
| D | THR185 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN E 300 |
| Chain | Residue |
| E | CYS186 |
| E | CYS195 |
| E | GLY196 |
| E | CYS198 |
| E | CYS201 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG E 400 |
| Chain | Residue |
| E | GLY13 |
| E | ASP15 |
| E | SER16 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 E 500 |
| Chain | Residue |
| E | GLY13 |
| E | GLN14 |
| E | ASP15 |
| E | LEU184 |
| E | THR185 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN F 300 |
| Chain | Residue |
| F | CYS186 |
| F | CYS195 |
| F | GLY196 |
| F | CYS198 |
| F | CYS201 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG F 400 |
| Chain | Residue |
| F | SER11 |
| F | GLY13 |
| F | ASP15 |
| F | SER16 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 F 500 |
| Chain | Residue |
| F | GLY13 |
| F | GLN14 |
| F | ASP15 |
| F | LYS163 |
| F | THR185 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 84 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18491386","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






