3BL5
Crystal structure of QueC from Bacillus subtilis: an enzyme involved in preQ1 biosynthesis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008616 | biological_process | queuosine 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 | 0005524 | molecular_function | ATP binding |
B | 0008270 | molecular_function | zinc ion binding |
B | 0008616 | biological_process | queuosine 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 | 0005524 | molecular_function | ATP binding |
C | 0008270 | molecular_function | zinc ion binding |
C | 0008616 | biological_process | queuosine 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 | 0005524 | molecular_function | ATP binding |
D | 0008270 | molecular_function | zinc ion binding |
D | 0008616 | biological_process | queuosine 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 | 0005524 | molecular_function | ATP binding |
E | 0008270 | molecular_function | zinc ion binding |
E | 0008616 | biological_process | queuosine 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 | 0005524 | molecular_function | ATP binding |
F | 0008270 | molecular_function | zinc ion binding |
F | 0008616 | biological_process | queuosine 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 | 30 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18491386 |
Chain | Residue | Details |
A | PHE10 | |
B | CYS201 | |
C | PHE10 | |
C | CYS186 | |
C | CYS195 | |
C | CYS198 | |
C | CYS201 | |
D | PHE10 | |
D | CYS186 | |
D | CYS195 | |
D | CYS198 | |
A | CYS186 | |
D | CYS201 | |
E | PHE10 | |
E | CYS186 | |
E | CYS195 | |
E | CYS198 | |
E | CYS201 | |
F | PHE10 | |
F | CYS186 | |
F | CYS195 | |
F | CYS198 | |
A | CYS195 | |
F | CYS201 | |
A | CYS198 | |
A | CYS201 | |
B | PHE10 | |
B | CYS186 | |
B | CYS195 | |
B | CYS198 |