4TVW
Resorufin ligase with bound resorufin-AMP analog
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0009249 | biological_process | protein lipoylation |
A | 0016874 | molecular_function | ligase activity |
A | 0016979 | molecular_function | lipoate-protein ligase activity |
A | 0017118 | molecular_function | lipoyltransferase activity |
A | 0036211 | biological_process | protein modification process |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0009249 | biological_process | protein lipoylation |
B | 0016874 | molecular_function | ligase activity |
B | 0016979 | molecular_function | lipoate-protein ligase activity |
B | 0017118 | molecular_function | lipoyltransferase activity |
B | 0036211 | biological_process | protein modification process |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0009249 | biological_process | protein lipoylation |
C | 0016874 | molecular_function | ligase activity |
C | 0016979 | molecular_function | lipoate-protein ligase activity |
C | 0017118 | molecular_function | lipoyltransferase activity |
C | 0036211 | biological_process | protein modification process |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0009249 | biological_process | protein lipoylation |
D | 0016874 | molecular_function | ligase activity |
D | 0016979 | molecular_function | lipoate-protein ligase activity |
D | 0017118 | molecular_function | lipoyltransferase activity |
D | 0036211 | biological_process | protein modification process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | binding site for residue 37P A 401 |
Chain | Residue |
A | ALA20 |
A | ASN83 |
A | LYS133 |
A | SER137 |
A | ALA138 |
A | ARG140 |
A | GLY149 |
A | THR151 |
A | LEU161 |
A | LEU165 |
A | SER179 |
A | TRP37 |
A | VAL180 |
A | SER182 |
A | ARG70 |
A | SER72 |
A | GLY75 |
A | ALA76 |
A | VAL77 |
A | PHE78 |
A | HIS79 |
site_id | AC2 |
Number of Residues | 23 |
Details | binding site for residue 37P B 401 |
Chain | Residue |
B | ALA20 |
B | ARG70 |
B | GLY75 |
B | ALA76 |
B | VAL77 |
B | PHE78 |
B | HIS79 |
B | ASN83 |
B | LYS133 |
B | GLY136 |
B | SER137 |
B | ALA138 |
B | ARG140 |
B | GLY149 |
B | THR151 |
B | LEU153 |
B | LEU161 |
B | LEU165 |
B | SER179 |
B | VAL180 |
B | ARG181 |
B | SER182 |
B | VAL184 |
site_id | AC3 |
Number of Residues | 22 |
Details | binding site for residue 37P C 401 |
Chain | Residue |
C | ALA20 |
C | TRP37 |
C | ARG70 |
C | SER72 |
C | GLY75 |
C | VAL77 |
C | PHE78 |
C | HIS79 |
C | ASN83 |
C | THR87 |
C | LYS133 |
C | GLY136 |
C | SER137 |
C | ALA138 |
C | GLY149 |
C | THR151 |
C | LEU153 |
C | LEU161 |
C | SER179 |
C | VAL180 |
C | ARG181 |
C | SER182 |
site_id | AC4 |
Number of Residues | 25 |
Details | binding site for residue 37P D 401 |
Chain | Residue |
D | LEU17 |
D | ALA20 |
D | TRP37 |
D | ARG70 |
D | SER72 |
D | GLY75 |
D | ALA76 |
D | VAL77 |
D | PHE78 |
D | HIS79 |
D | ASN83 |
D | ASN121 |
D | LYS133 |
D | SER137 |
D | ALA138 |
D | GLY149 |
D | THR151 |
D | LEU153 |
D | LEU161 |
D | LEU165 |
D | SER179 |
D | VAL180 |
D | ARG181 |
D | SER182 |
D | VAL184 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ARG70 | |
D | ARG70 | |
D | GLY75 | |
D | LYS133 | |
A | GLY75 | |
A | LYS133 | |
B | ARG70 | |
B | GLY75 | |
B | LYS133 | |
C | ARG70 | |
C | GLY75 | |
C | LYS133 |