6YJ2
Structural and DNA binding studies of the transcriptional repressor Rv2506 (BkaR) from Mycobacterium tuberculosis supports a role in L-Leucine catabolism
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000976 | molecular_function | transcription cis-regulatory region binding |
A | 0003677 | molecular_function | DNA binding |
A | 0003700 | molecular_function | DNA-binding transcription factor activity |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0042783 | biological_process | evasion of host immune response |
A | 0042802 | molecular_function | identical protein binding |
B | 0000976 | molecular_function | transcription cis-regulatory region binding |
B | 0003677 | molecular_function | DNA binding |
B | 0003700 | molecular_function | DNA-binding transcription factor activity |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0042783 | biological_process | evasion of host immune response |
B | 0042802 | molecular_function | identical protein binding |
C | 0000976 | molecular_function | transcription cis-regulatory region binding |
C | 0003677 | molecular_function | DNA binding |
C | 0003700 | molecular_function | DNA-binding transcription factor activity |
C | 0006355 | biological_process | regulation of DNA-templated transcription |
C | 0042783 | biological_process | evasion of host immune response |
C | 0042802 | molecular_function | identical protein binding |
D | 0000976 | molecular_function | transcription cis-regulatory region binding |
D | 0003677 | molecular_function | DNA binding |
D | 0003700 | molecular_function | DNA-binding transcription factor activity |
D | 0006355 | biological_process | regulation of DNA-templated transcription |
D | 0042783 | biological_process | evasion of host immune response |
D | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue GOL B 301 |
Chain | Residue |
B | HIS109 |
B | GLN123 |
B | GLN142 |
B | ASN177 |
B | HOH417 |
B | HOH419 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue GOL B 302 |
Chain | Residue |
B | GLU116 |
B | HOH431 |
B | ARG83 |
B | LEU84 |
B | PHE108 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue GOL B 303 |
Chain | Residue |
B | ILE120 |
B | ARG121 |
B | ASP124 |
B | ASN177 |
B | PRO180 |
B | HIS181 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue GOL D 301 |
Chain | Residue |
D | ARG83 |
D | PHE108 |
D | GLU116 |
D | HOH451 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue GOL D 302 |
Chain | Residue |
C | SER178 |
C | HIS181 |
C | HOH422 |
D | HIS170 |
D | ASN177 |
D | HOH410 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue GOL A 301 |
Chain | Residue |
A | ARG83 |
A | PHE108 |
A | PHE112 |
A | GLU116 |
A | HOH402 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue GOL C 301 |
Chain | Residue |
C | VAL194 |
C | ARG195 |
C | ALA198 |
D | GLU147 |
D | HOH417 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue GOL C 302 |
Chain | Residue |
C | GLU107 |
C | ASP111 |
C | ARG197 |
C | HOH405 |
C | HOH426 |
C | HOH431 |
D | ARG154 |
D | PRO158 |
D | GLY159 |