6HSD
Crystal structure of the oxidized form of the transcription regulator RsrR
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003700 | molecular_function | DNA-binding transcription factor activity |
A | 0005829 | cellular_component | cytosol |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0046872 | molecular_function | metal ion binding |
A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
B | 0003700 | molecular_function | DNA-binding transcription factor activity |
B | 0005829 | cellular_component | cytosol |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0046872 | molecular_function | metal ion binding |
B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
C | 0003700 | molecular_function | DNA-binding transcription factor activity |
C | 0005829 | cellular_component | cytosol |
C | 0006355 | biological_process | regulation of DNA-templated transcription |
C | 0046872 | molecular_function | metal ion binding |
C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
D | 0003700 | molecular_function | DNA-binding transcription factor activity |
D | 0005829 | cellular_component | cytosol |
D | 0006355 | biological_process | regulation of DNA-templated transcription |
D | 0046872 | molecular_function | metal ion binding |
D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue FES A 201 |
Chain | Residue |
A | GLU8 |
A | HIS12 |
C | CYS90 |
C | GLU92 |
C | ILE93 |
C | ARG94 |
C | CYS110 |
C | ILE112 |
C | ALA113 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue MES A 202 |
Chain | Residue |
A | GLY5 |
A | TRP9 |
A | TYR39 |
A | HOH303 |
A | HOH343 |
A | HOH419 |
A | HOH460 |
A | HOH466 |
A | HOH468 |
C | HOH409 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue GOL A 203 |
Chain | Residue |
A | HIS12 |
A | GOL206 |
C | ARG94 |
C | MES202 |
C | GOL206 |
C | HOH307 |
C | HOH317 |
C | HOH411 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue GOL A 204 |
Chain | Residue |
A | GLN79 |
A | PRO84 |
A | ASP85 |
A | PRO86 |
A | ALA87 |
A | GLU120 |
A | TRP123 |
A | ARG124 |
A | HOH318 |
C | MET1 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue GOL A 205 |
Chain | Residue |
A | LYS59 |
A | HIS161 |
A | HIS162 |
A | HIS163 |
A | HOH382 |
D | GLY150 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue GOL A 206 |
Chain | Residue |
A | SER143 |
A | VAL151 |
A | GOL203 |
A | HOH370 |
C | LEU99 |
C | THR101 |
C | MES202 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue GOL A 207 |
Chain | Residue |
A | ALA27 |
A | HOH384 |
site_id | AC8 |
Number of Residues | 8 |
Details | binding site for residue FES B 201 |
Chain | Residue |
B | GLU8 |
B | HIS12 |
D | CYS90 |
D | GLU92 |
D | ILE93 |
D | ARG94 |
D | CYS110 |
D | ALA113 |
site_id | AC9 |
Number of Residues | 11 |
Details | binding site for residue GOL B 202 |
Chain | Residue |
B | HIS12 |
B | VAL16 |
B | HIS33 |
B | HOH305 |
B | HOH335 |
B | HOH342 |
B | HOH360 |
B | HOH374 |
D | LEU99 |
D | MES202 |
D | HOH304 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue GOL B 203 |
Chain | Residue |
A | ARG124 |
A | HOH342 |
A | HOH371 |
B | SER38 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue FES C 201 |
Chain | Residue |
A | CYS90 |
A | ILE93 |
A | ARG94 |
A | CYS110 |
A | ILE112 |
A | ALA113 |
C | GLU8 |
C | HIS12 |
site_id | AD3 |
Number of Residues | 14 |
Details | binding site for residue MES C 202 |
Chain | Residue |
A | HIS33 |
A | SER143 |
A | VAL151 |
A | GOL203 |
A | GOL206 |
A | HOH445 |
C | ARG94 |
C | ARG96 |
C | LEU99 |
C | THR101 |
C | HOH306 |
C | HOH307 |
C | HOH320 |
C | HOH411 |
site_id | AD4 |
Number of Residues | 10 |
Details | binding site for residue GOL C 203 |
Chain | Residue |
C | GLY83 |
C | PRO84 |
C | ASP85 |
C | ALA87 |
C | GLU120 |
C | TRP123 |
C | ARG124 |
C | HOH330 |
A | MET1 |
C | GLN79 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue GOL C 204 |
Chain | Residue |
A | GLN57 |
C | GLN95 |
C | THR101 |
C | PRO103 |
C | HOH304 |
site_id | AD6 |
Number of Residues | 7 |
Details | binding site for residue GOL C 205 |
Chain | Residue |
A | ARG94 |
A | HOH308 |
C | HIS12 |
C | VAL15 |
C | VAL16 |
C | GOL207 |
C | HOH305 |
site_id | AD7 |
Number of Residues | 8 |
Details | binding site for residue GOL C 206 |
Chain | Residue |
A | GLU142 |
A | GOL203 |
C | ARG94 |
C | LYS105 |
C | LYS108 |
C | PRO111 |
C | HOH310 |
C | HOH317 |
site_id | AD8 |
Number of Residues | 7 |
Details | binding site for residue GOL C 207 |
Chain | Residue |
A | LEU99 |
A | THR101 |
C | HIS12 |
C | VAL16 |
C | HIS33 |
C | GOL205 |
C | HOH301 |
site_id | AD9 |
Number of Residues | 1 |
Details | binding site for residue CL C 208 |
Chain | Residue |
C | ALA69 |
site_id | AE1 |
Number of Residues | 8 |
Details | binding site for residue FES D 201 |
Chain | Residue |
B | CYS90 |
B | GLU92 |
B | ILE93 |
B | ARG94 |
B | CYS110 |
B | ALA113 |
D | GLU8 |
D | HIS12 |
site_id | AE2 |
Number of Residues | 8 |
Details | binding site for residue MES D 202 |
Chain | Residue |
B | HIS12 |
B | SER143 |
B | GOL202 |
B | HOH331 |
B | HOH374 |
D | ARG94 |
D | THR101 |
D | HOH304 |
site_id | AE3 |
Number of Residues | 6 |
Details | binding site for residue GOL D 203 |
Chain | Residue |
B | ARG94 |
D | HIS12 |
D | VAL15 |
D | VAL16 |
D | HOH301 |
D | HOH307 |
site_id | AE4 |
Number of Residues | 9 |
Details | binding site for residue GOL D 204 |
Chain | Residue |
B | HOH318 |
D | VAL78 |
D | GLN79 |
D | ASP82 |
D | GLY83 |
D | ASP85 |
D | GLU120 |
D | TRP123 |
D | ARG124 |
site_id | AE5 |
Number of Residues | 4 |
Details | binding site for residue CL D 205 |
Chain | Residue |
D | ALA87 |
D | PHE88 |
D | VAL89 |
D | HOH305 |
Functional Information from PROSITE/UniProt
site_id | PS01332 |
Number of Residues | 19 |
Details | HTH_RRF2_1 Rrf2-type HTH domain signature. LsraGLvrSvqGktGGYvL |
Chain | Residue | Details |
A | LEU47-LEU65 |