2ZFZ
Crystal structure of the C-terminal domain hexamer of ArgR from Mycobacterium tuberculosis in complex with arginine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003700 | molecular_function | DNA-binding transcription factor activity |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0034618 | molecular_function | arginine binding |
A | 0051259 | biological_process | protein complex oligomerization |
B | 0003700 | molecular_function | DNA-binding transcription factor activity |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0034618 | molecular_function | arginine binding |
B | 0051259 | biological_process | protein complex oligomerization |
C | 0003700 | molecular_function | DNA-binding transcription factor activity |
C | 0006355 | biological_process | regulation of DNA-templated transcription |
C | 0034618 | molecular_function | arginine binding |
C | 0051259 | biological_process | protein complex oligomerization |
D | 0003700 | molecular_function | DNA-binding transcription factor activity |
D | 0006355 | biological_process | regulation of DNA-templated transcription |
D | 0034618 | molecular_function | arginine binding |
D | 0051259 | biological_process | protein complex oligomerization |
E | 0003700 | molecular_function | DNA-binding transcription factor activity |
E | 0006355 | biological_process | regulation of DNA-templated transcription |
E | 0034618 | molecular_function | arginine binding |
E | 0051259 | biological_process | protein complex oligomerization |
F | 0003700 | molecular_function | DNA-binding transcription factor activity |
F | 0006355 | biological_process | regulation of DNA-templated transcription |
F | 0034618 | molecular_function | arginine binding |
F | 0051259 | biological_process | protein complex oligomerization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ARG A 300 |
Chain | Residue |
A | HIS125 |
C | ASP146 |
C | ASP147 |
C | THR148 |
F | PRO121 |
F | GLY122 |
F | ASP146 |
A | ALA128 |
A | ASP132 |
A | THR142 |
A | ILE143 |
A | ALA144 |
A | HOH508 |
A | HOH512 |
C | GLY145 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ARG B 300 |
Chain | Residue |
A | GLY145 |
A | ASP146 |
A | ASP147 |
A | THR148 |
B | HIS125 |
B | ALA128 |
B | ASP132 |
B | THR142 |
B | ILE143 |
B | ALA144 |
B | HOH534 |
B | HOH547 |
E | GLY122 |
E | ASP146 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ARG C 300 |
Chain | Residue |
B | ARG118 |
B | GLY145 |
B | ASP146 |
B | ASP147 |
B | THR148 |
C | HIS125 |
C | ALA128 |
C | ASP132 |
C | THR142 |
C | ILE143 |
C | ALA144 |
C | HOH507 |
C | HOH508 |
D | PRO121 |
D | GLY122 |
D | ASP146 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ARG D 300 |
Chain | Residue |
C | GLY122 |
C | ASP146 |
D | HIS125 |
D | ALA128 |
D | ASP132 |
D | THR142 |
D | ILE143 |
D | ALA144 |
D | HOH568 |
D | HOH579 |
F | GLY145 |
F | ASP146 |
F | ASP147 |
F | THR148 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ARG E 300 |
Chain | Residue |
B | PRO121 |
B | ASP146 |
D | GLY145 |
D | ASP146 |
D | ASP147 |
D | THR148 |
E | HIS125 |
E | ALA128 |
E | ASP132 |
E | THR142 |
E | ILE143 |
E | ALA144 |
E | HOH583 |
E | HOH586 |
site_id | AC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ARG F 300 |
Chain | Residue |
A | PRO121 |
A | ASP146 |
E | GLY145 |
E | ASP146 |
E | ASP147 |
E | THR148 |
F | HIS125 |
F | ALA128 |
F | ASP132 |
F | THR142 |
F | ILE143 |
F | ALA144 |
F | HOH507 |
F | HOH512 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GAI A 400 |
Chain | Residue |
A | GLY164 |
A | GLU167 |
A | ASN168 |
E | GLY102 |
E | GLU103 |
E | LEU105 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GAI E 400 |
Chain | Residue |
A | LEU105 |
A | VAL106 |
A | GLU167 |
A | ARG170 |
A | HOH551 |