3B6A
Crystal structure of the Streptomyces coelicolor TetR family protein ActR in complex with actinorhodin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
A | 0046677 | biological_process | response to antibiotic |
B | 0003677 | molecular_function | DNA binding |
B | 0045892 | biological_process | negative regulation of DNA-templated transcription |
B | 0046677 | biological_process | response to antibiotic |
C | 0003677 | molecular_function | DNA binding |
C | 0045892 | biological_process | negative regulation of DNA-templated transcription |
C | 0046677 | biological_process | response to antibiotic |
D | 0003677 | molecular_function | DNA binding |
D | 0045892 | biological_process | negative regulation of DNA-templated transcription |
D | 0046677 | biological_process | response to antibiotic |
E | 0003677 | molecular_function | DNA binding |
E | 0045892 | biological_process | negative regulation of DNA-templated transcription |
E | 0046677 | biological_process | response to antibiotic |
F | 0003677 | molecular_function | DNA binding |
F | 0045892 | biological_process | negative regulation of DNA-templated transcription |
F | 0046677 | biological_process | response to antibiotic |
G | 0003677 | molecular_function | DNA binding |
G | 0045892 | biological_process | negative regulation of DNA-templated transcription |
G | 0046677 | biological_process | response to antibiotic |
H | 0003677 | molecular_function | DNA binding |
H | 0045892 | biological_process | negative regulation of DNA-templated transcription |
H | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ZCT A 1 |
Chain | Residue |
A | LEU87 |
A | VAL137 |
A | GLY138 |
A | MET139 |
A | ASP161 |
A | SER164 |
A | VAL90 |
A | VAL92 |
A | LEU111 |
A | ALA125 |
A | ILE126 |
A | PRO130 |
A | ASN134 |
A | GLY135 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ZCT B 1 |
Chain | Residue |
A | GLU173 |
B | LEU87 |
B | VAL90 |
B | VAL92 |
B | LEU111 |
B | ALA125 |
B | ILE126 |
B | ARG128 |
B | PRO130 |
B | ASN134 |
B | GLY135 |
B | GLY138 |
B | MET139 |
B | ASP161 |
B | SER164 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ZCT C 1 |
Chain | Residue |
C | LEU87 |
C | VAL90 |
C | VAL92 |
C | LEU111 |
C | ALA125 |
C | ILE126 |
C | PRO130 |
C | GLY138 |
C | THR142 |
C | SER164 |
C | THR168 |
D | LEU172 |
D | GLU173 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ZCT D 1 |
Chain | Residue |
C | GLU173 |
D | LEU87 |
D | VAL90 |
D | VAL92 |
D | LEU111 |
D | ALA125 |
D | ILE126 |
D | ARG128 |
D | PRO130 |
D | ASN134 |
D | GLY135 |
D | GLY138 |
D | MET139 |
D | ASP161 |
D | SER164 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ZCT E 1 |
Chain | Residue |
E | LEU87 |
E | VAL90 |
E | GLU91 |
E | VAL92 |
E | LEU111 |
E | ALA125 |
E | ILE126 |
E | ARG128 |
E | PRO130 |
E | ASN134 |
E | GLY135 |
E | GLY138 |
E | ASP161 |
E | SER164 |
site_id | AC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ZCT F 1 |
Chain | Residue |
F | LEU87 |
F | VAL90 |
F | GLU91 |
F | VAL92 |
F | ALA125 |
F | ILE126 |
F | ARG128 |
F | PRO130 |
F | ASN134 |
F | GLY135 |
F | GLY138 |
F | MET139 |
F | ARG141 |
F | SER164 |
site_id | AC7 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ZCT G 1 |
Chain | Residue |
G | LEU87 |
G | VAL90 |
G | VAL92 |
G | LEU111 |
G | ALA125 |
G | ILE126 |
G | PRO130 |
G | ASN134 |
G | GLY135 |
G | VAL137 |
G | GLY138 |
G | MET139 |
G | ASP161 |
G | SER164 |
site_id | AC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ZCT H 1 |
Chain | Residue |
H | LEU87 |
H | VAL90 |
H | VAL92 |
H | LEU111 |
H | ALA125 |
H | ARG128 |
H | PRO130 |
H | ASN134 |
H | GLY135 |
H | GLY138 |
H | MET139 |
H | SER164 |