6HSM
Structure of partially reduced RsrR in space group P2(1)2(1)2(1)
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 |
E | 0003700 | molecular_function | DNA-binding transcription factor activity |
E | 0005829 | cellular_component | cytosol |
E | 0006355 | biological_process | regulation of DNA-templated transcription |
E | 0046872 | molecular_function | metal ion binding |
E | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
F | 0003700 | molecular_function | DNA-binding transcription factor activity |
F | 0005829 | cellular_component | cytosol |
F | 0006355 | biological_process | regulation of DNA-templated transcription |
F | 0046872 | molecular_function | metal ion binding |
F | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
G | 0003700 | molecular_function | DNA-binding transcription factor activity |
G | 0005829 | cellular_component | cytosol |
G | 0006355 | biological_process | regulation of DNA-templated transcription |
G | 0046872 | molecular_function | metal ion binding |
G | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
H | 0003700 | molecular_function | DNA-binding transcription factor activity |
H | 0005829 | cellular_component | cytosol |
H | 0006355 | biological_process | regulation of DNA-templated transcription |
H | 0046872 | molecular_function | metal ion binding |
H | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue FES A 201 |
Chain | Residue |
A | GLU8 |
A | HIS12 |
D | CYS90 |
D | ILE93 |
D | ARG94 |
D | CYS110 |
D | ALA113 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MPD A 202 |
Chain | Residue |
A | GLU157 |
A | MPD205 |
A | HOH309 |
A | HOH347 |
A | GLY150 |
A | ALA153 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue MPD A 203 |
Chain | Residue |
A | HIS12 |
A | VAL139 |
D | THR101 |
D | CYS110 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue MPD A 204 |
Chain | Residue |
A | ARG94 |
D | HIS12 |
D | VAL139 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue MPD A 205 |
Chain | Residue |
A | MPD202 |
B | ALA125 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue MPD A 206 |
Chain | Residue |
A | VAL35 |
E | TRP154 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue MPD A 207 |
Chain | Residue |
A | SER21 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue GOL A 208 |
Chain | Residue |
A | ASP85 |
A | GLU120 |
A | TRP123 |
A | ARG124 |
A | HOH328 |
D | MET1 |
D | HOH332 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue FES A 209 |
Chain | Residue |
A | CYS90 |
A | ILE93 |
A | ARG94 |
A | CYS110 |
A | ALA113 |
D | GLU8 |
D | HIS12 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue MPD D 201 |
Chain | Residue |
A | PRO98 |
D | TRP154 |
site_id | AD2 |
Number of Residues | 1 |
Details | binding site for residue MPD D 202 |
Chain | Residue |
D | ALA113 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue MPD D 203 |
Chain | Residue |
D | SER48 |
D | GLY51 |
D | VAL53 |
D | SER55 |
D | THR66 |
H | LEU65 |
H | ARG67 |
H | PRO68 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue MPD D 204 |
Chain | Residue |
B | THR18 |
B | ALA20 |
B | SER21 |
D | ALA122 |
D | ALA125 |
D | SER126 |
D | HOH379 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue MPD D 205 |
Chain | Residue |
A | ALA115 |
D | LEU135 |
D | THR138 |
site_id | AD6 |
Number of Residues | 7 |
Details | binding site for residue MPD D 206 |
Chain | Residue |
A | ILE93 |
D | VAL35 |
D | TYR39 |
D | GOL207 |
D | HOH366 |
D | HOH367 |
D | HOH374 |
site_id | AD7 |
Number of Residues | 10 |
Details | binding site for residue GOL D 207 |
Chain | Residue |
D | SER4 |
D | GLY5 |
D | TYR39 |
D | MPD206 |
D | HOH325 |
D | HOH381 |
E | SER4 |
E | GLY5 |
E | HOH318 |
E | HOH374 |
site_id | AD8 |
Number of Residues | 2 |
Details | binding site for residue CL D 208 |
Chain | Residue |
D | LYS108 |
D | ALA109 |
site_id | AD9 |
Number of Residues | 7 |
Details | binding site for residue FES B 201 |
Chain | Residue |
B | GLU8 |
B | HIS12 |
C | CYS90 |
C | ILE93 |
C | ARG94 |
C | CYS110 |
C | ALA113 |
site_id | AE1 |
Number of Residues | 5 |
Details | binding site for residue MPD B 202 |
Chain | Residue |
B | HIS12 |
B | VAL139 |
B | HOH340 |
C | ARG94 |
C | THR101 |
site_id | AE2 |
Number of Residues | 2 |
Details | binding site for residue MPD B 203 |
Chain | Residue |
B | GLY150 |
B | GLU157 |
site_id | AE3 |
Number of Residues | 5 |
Details | binding site for residue MPD B 204 |
Chain | Residue |
B | ARG94 |
B | CYS110 |
B | HOH313 |
B | HOH333 |
C | HIS12 |
site_id | AE4 |
Number of Residues | 3 |
Details | binding site for residue MPD B 205 |
Chain | Residue |
A | ALA128 |
B | ASP146 |
A | ARG124 |
site_id | AE5 |
Number of Residues | 8 |
Details | binding site for residue MPD B 206 |
Chain | Residue |
B | MET1 |
B | ALA87 |
B | GLU120 |
B | TRP123 |
B | HOH360 |
C | ALA87 |
C | GLU120 |
C | TRP123 |
site_id | AE6 |
Number of Residues | 3 |
Details | binding site for residue MPD B 207 |
Chain | Residue |
B | ASP34 |
B | VAL35 |
B | HOH336 |
site_id | AE7 |
Number of Residues | 2 |
Details | binding site for residue CL B 208 |
Chain | Residue |
B | PRO68 |
B | ALA69 |
site_id | AE8 |
Number of Residues | 4 |
Details | binding site for residue MG B 209 |
Chain | Residue |
B | LEU159 |
B | HIS163 |
B | HOH335 |
C | ASP134 |
site_id | AE9 |
Number of Residues | 7 |
Details | binding site for residue FES B 210 |
Chain | Residue |
B | CYS90 |
B | ILE93 |
B | ARG94 |
B | CYS110 |
B | ALA113 |
C | GLU8 |
C | HIS12 |
site_id | AF1 |
Number of Residues | 7 |
Details | binding site for residue MPD C 201 |
Chain | Residue |
C | SER4 |
C | GLY5 |
C | GLY6 |
C | TYR39 |
C | GLN43 |
F | SER4 |
F | GLY5 |
site_id | AF2 |
Number of Residues | 2 |
Details | binding site for residue MPD C 202 |
Chain | Residue |
C | ARG49 |
E | ARG54 |
site_id | AF3 |
Number of Residues | 7 |
Details | binding site for residue GOL C 203 |
Chain | Residue |
B | GLU142 |
B | SER143 |
C | ARG94 |
C | LYS105 |
C | CYS106 |
C | THR107 |
C | LYS108 |
site_id | AF4 |
Number of Residues | 8 |
Details | binding site for residue FES E 201 |
Chain | Residue |
E | CYS90 |
E | GLU92 |
E | ILE93 |
E | ARG94 |
E | CYS110 |
E | ALA113 |
G | GLU8 |
G | HIS12 |
site_id | AF5 |
Number of Residues | 7 |
Details | binding site for residue FES E 202 |
Chain | Residue |
E | GLU8 |
E | HIS12 |
G | CYS90 |
G | ILE93 |
G | ARG94 |
G | CYS110 |
G | ALA113 |
site_id | AF6 |
Number of Residues | 3 |
Details | binding site for residue MPD E 203 |
Chain | Residue |
E | HIS12 |
E | SER143 |
E | HOH302 |
site_id | AF7 |
Number of Residues | 5 |
Details | binding site for residue GOL E 204 |
Chain | Residue |
E | ALA26 |
E | SER55 |
E | GLY62 |
E | TYR63 |
E | HOH338 |
site_id | AF8 |
Number of Residues | 10 |
Details | binding site for residue MES E 205 |
Chain | Residue |
A | MET1 |
A | LYS2 |
D | ASP82 |
E | VAL35 |
E | SER36 |
E | TYR39 |
E | HOH322 |
E | HOH329 |
E | HOH339 |
G | ILE93 |
site_id | AF9 |
Number of Residues | 4 |
Details | binding site for residue MPD G 201 |
Chain | Residue |
E | THR138 |
G | PRO111 |
G | HOH305 |
G | HOH315 |
site_id | AG1 |
Number of Residues | 3 |
Details | binding site for residue MPD G 202 |
Chain | Residue |
G | GLN57 |
G | ALA109 |
G | ALA113 |
site_id | AG2 |
Number of Residues | 3 |
Details | binding site for residue MPD G 203 |
Chain | Residue |
G | ARG54 |
G | THR66 |
G | GLN95 |
site_id | AG3 |
Number of Residues | 8 |
Details | binding site for residue FES F 201 |
Chain | Residue |
F | GLU8 |
F | HIS12 |
H | CYS90 |
H | GLU92 |
H | ILE93 |
H | ARG94 |
H | CYS110 |
H | ALA113 |
site_id | AG4 |
Number of Residues | 2 |
Details | binding site for residue MPD F 202 |
Chain | Residue |
F | HIS12 |
F | VAL139 |
site_id | AG5 |
Number of Residues | 7 |
Details | binding site for residue MPD F 203 |
Chain | Residue |
C | TRP9 |
C | TYR39 |
F | MET1 |
F | LYS2 |
F | HOH303 |
F | HOH330 |
H | LYS2 |
site_id | AG6 |
Number of Residues | 2 |
Details | binding site for residue GOL F 204 |
Chain | Residue |
F | TRP154 |
H | PRO98 |
site_id | AG7 |
Number of Residues | 1 |
Details | binding site for residue CL F 205 |
Chain | Residue |
F | ALA69 |
site_id | AG8 |
Number of Residues | 8 |
Details | binding site for residue FES F 206 |
Chain | Residue |
F | CYS90 |
F | GLU92 |
F | ILE93 |
F | ARG94 |
F | CYS110 |
F | ALA113 |
H | GLU8 |
H | HIS12 |
site_id | AG9 |
Number of Residues | 1 |
Details | binding site for residue MPD H 201 |
Chain | Residue |
H | HIS12 |
site_id | AH1 |
Number of Residues | 5 |
Details | binding site for residue MPD H 202 |
Chain | Residue |
F | MET1 |
H | ASP85 |
H | ALA87 |
H | GLU120 |
H | TRP123 |
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 |