2Q2A
Crystal structures of the arginine-, lysine-, histidine-binding protein ArtJ from the thermophilic bacterium Geobacillus stearothermophilus
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005886 | cellular_component | plasma membrane |
A | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
A | 0016020 | cellular_component | membrane |
A | 0034220 | biological_process | monoatomic ion transmembrane transport |
B | 0005886 | cellular_component | plasma membrane |
B | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
B | 0016020 | cellular_component | membrane |
B | 0034220 | biological_process | monoatomic ion transmembrane transport |
C | 0005886 | cellular_component | plasma membrane |
C | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
C | 0016020 | cellular_component | membrane |
C | 0034220 | biological_process | monoatomic ion transmembrane transport |
D | 0005886 | cellular_component | plasma membrane |
D | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
D | 0016020 | cellular_component | membrane |
D | 0034220 | biological_process | monoatomic ion transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 903 |
Chain | Residue |
A | LYS242 |
A | LYS245 |
A | ARG248 |
A | HOH1035 |
A | HOH1047 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 902 |
Chain | Residue |
B | LYS242 |
B | LYS245 |
B | ARG248 |
B | HOH1052 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 901 |
Chain | Residue |
C | LYS242 |
C | LYS245 |
C | ARG248 |
C | HOH965 |
C | HOH1107 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 904 |
Chain | Residue |
D | LYS242 |
D | LYS245 |
D | ARG248 |
D | HOH1030 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ARG A 904 |
Chain | Residue |
A | ASP28 |
A | PHE31 |
A | GLU35 |
A | TRP68 |
A | SER85 |
A | GLY86 |
A | ILE87 |
A | THR88 |
A | ARG93 |
A | GLN132 |
A | THR135 |
A | THR136 |
A | ASP175 |
A | TYR205 |
site_id | AC6 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ARG B 903 |
Chain | Residue |
B | ASP28 |
B | PHE31 |
B | GLU35 |
B | TRP68 |
B | SER85 |
B | GLY86 |
B | ILE87 |
B | THR88 |
B | ARG93 |
B | GLN132 |
B | THR135 |
B | THR136 |
B | ASP175 |
site_id | AC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ARG C 902 |
Chain | Residue |
C | ASP28 |
C | PHE31 |
C | GLU35 |
C | TRP68 |
C | SER85 |
C | GLY86 |
C | ILE87 |
C | THR88 |
C | ARG93 |
C | GLN132 |
C | THR135 |
C | THR136 |
C | ASP175 |
site_id | AC8 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ARG D 905 |
Chain | Residue |
D | ASP28 |
D | PHE31 |
D | GLU35 |
D | TRP68 |
D | SER85 |
D | GLY86 |
D | ILE87 |
D | THR88 |
D | ARG93 |
D | GLN132 |
D | THR135 |
D | THR136 |
D | ASP175 |