6Y45
Crystal Structure of the H33A variant of 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 | 0046872 | molecular_function | metal ion binding |
A | 0051536 | molecular_function | iron-sulfur cluster 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 | 0046872 | molecular_function | metal ion binding |
B | 0051536 | molecular_function | iron-sulfur cluster 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 | 0046872 | molecular_function | metal ion binding |
C | 0051536 | molecular_function | iron-sulfur cluster 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 | 0046872 | molecular_function | metal ion binding |
D | 0051536 | molecular_function | iron-sulfur cluster binding |
D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
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 | ALA113 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue MPD A 202 |
Chain | Residue |
A | VAL151 |
A | MPD204 |
A | HOH311 |
A | HIS12 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue MPD A 203 |
Chain | Residue |
A | VAL78 |
A | ASP85 |
A | ALA87 |
A | GLU120 |
A | TRP123 |
A | HOH376 |
C | LYS2 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue MPD A 204 |
Chain | Residue |
A | HIS12 |
A | LEU32 |
A | MPD202 |
A | HOH311 |
C | ILE93 |
site_id | AC5 |
Number of Residues | 9 |
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 | ILE112 |
D | ALA113 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue MPD B 202 |
Chain | Residue |
B | HIS12 |
B | MPD205 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue SO4 B 203 |
Chain | Residue |
B | HOH340 |
site_id | AC8 |
Number of Residues | 1 |
Details | binding site for residue NA B 204 |
Chain | Residue |
B | TRP123 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue MPD B 205 |
Chain | Residue |
B | HIS12 |
B | VAL16 |
B | LEU32 |
B | MPD202 |
D | ILE93 |
D | ARG94 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue MPD B 206 |
Chain | Residue |
B | ILE93 |
B | LEU99 |
D | HIS12 |
D | LEU32 |
D | MPD403 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue FES C 201 |
Chain | Residue |
A | CYS90 |
A | GLU92 |
A | ILE93 |
A | ARG94 |
A | CYS110 |
A | ALA113 |
C | GLU8 |
C | HIS12 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue MPD C 202 |
Chain | Residue |
A | ARG94 |
C | HIS12 |
C | HOH351 |
site_id | AD4 |
Number of Residues | 9 |
Details | binding site for residue FES D 402 |
Chain | Residue |
B | CYS90 |
B | GLU92 |
B | ILE93 |
B | ARG94 |
B | CYS110 |
B | ILE112 |
B | ALA113 |
D | GLU8 |
D | HIS12 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue MPD D 403 |
Chain | Residue |
B | ARG94 |
B | THR101 |
B | MPD206 |
B | HOH370 |
D | HIS12 |
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 |