2WV0
Crystal structure of the GntR-HutC family member YvoA from Bacillus subtilis
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0045892 | biological_process | negative regulation of DNA-templated transcription |
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 | 0045892 | biological_process | negative regulation of DNA-templated transcription |
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 | 0045892 | biological_process | negative regulation of DNA-templated transcription |
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 | 0045892 | biological_process | negative regulation of DNA-templated transcription |
E | 0003677 | molecular_function | DNA binding |
E | 0003700 | molecular_function | DNA-binding transcription factor activity |
E | 0006355 | biological_process | regulation of DNA-templated transcription |
E | 0045892 | biological_process | negative regulation of DNA-templated transcription |
F | 0003677 | molecular_function | DNA binding |
F | 0003700 | molecular_function | DNA-binding transcription factor activity |
F | 0006355 | biological_process | regulation of DNA-templated transcription |
F | 0045892 | biological_process | negative regulation of DNA-templated transcription |
G | 0003677 | molecular_function | DNA binding |
G | 0003700 | molecular_function | DNA-binding transcription factor activity |
G | 0006355 | biological_process | regulation of DNA-templated transcription |
G | 0045892 | biological_process | negative regulation of DNA-templated transcription |
H | 0003677 | molecular_function | DNA binding |
H | 0003700 | molecular_function | DNA-binding transcription factor activity |
H | 0006355 | biological_process | regulation of DNA-templated transcription |
H | 0045892 | biological_process | negative regulation of DNA-templated transcription |
I | 0003677 | molecular_function | DNA binding |
I | 0003700 | molecular_function | DNA-binding transcription factor activity |
I | 0006355 | biological_process | regulation of DNA-templated transcription |
I | 0045892 | biological_process | negative regulation of DNA-templated transcription |
J | 0003677 | molecular_function | DNA binding |
J | 0003700 | molecular_function | DNA-binding transcription factor activity |
J | 0006355 | biological_process | regulation of DNA-templated transcription |
J | 0045892 | biological_process | negative regulation of DNA-templated transcription |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 I 1243 |
Chain | Residue |
A | GLN108 |
A | LYS130 |
I | PRO10 |
I | ILE11 |
I | TYR12 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 1243 |
Chain | Residue |
D | GLN108 |
D | LYS130 |
B | PRO10 |
B | ILE11 |
B | TYR12 |
B | THR50 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 1243 |
Chain | Residue |
B | GLN108 |
B | LYS130 |
D | PRO10 |
D | ILE11 |
D | TYR12 |
D | THR50 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 B 1244 |
Chain | Residue |
B | SER88 |
B | PHE89 |
B | THR90 |
B | ARG133 |
B | ARG135 |
B | SER165 |
B | ILE166 |
B | TYR167 |
B | HOH2098 |
B | HOH2109 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 C 1243 |
Chain | Residue |
C | PRO10 |
C | ILE11 |
C | TYR12 |
C | THR50 |
F | GLN108 |
F | LYS130 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 F 1243 |
Chain | Residue |
C | GLN108 |
C | LYS130 |
F | PRO10 |
F | ILE11 |
F | TYR12 |
F | THR50 |
F | HOH2092 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 G 1243 |
Chain | Residue |
E | GLN108 |
G | PRO10 |
G | ILE11 |
G | TYR12 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 C 1244 |
Chain | Residue |
C | SER88 |
C | PHE89 |
C | THR90 |
C | ARG133 |
C | ARG135 |
C | SER165 |
C | ILE166 |
C | TYR167 |
C | HOH2103 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 D 1244 |
Chain | Residue |
D | SER88 |
D | PHE89 |
D | THR90 |
D | ARG133 |
D | ARG135 |
D | SER164 |
D | SER165 |
D | ILE166 |
D | TYR167 |
D | HOH2113 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 E 1243 |
Chain | Residue |
E | SER88 |
E | PHE89 |
E | THR90 |
E | ARG133 |
E | ARG135 |
E | SER164 |
E | SER165 |
E | ILE166 |
E | TYR167 |
E | HOH2050 |
site_id | BC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 F 1244 |
Chain | Residue |
F | SER88 |
F | PHE89 |
F | THR90 |
F | ARG133 |
F | ARG135 |
F | SER165 |
F | ILE166 |
F | TYR167 |
F | HOH2093 |
site_id | BC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 G 1244 |
Chain | Residue |
G | SER88 |
G | PHE89 |
G | THR90 |
G | ARG133 |
G | ARG135 |
G | SER165 |
G | ILE166 |
G | TYR167 |
G | HOH2038 |
site_id | BC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 I 1244 |
Chain | Residue |
I | TYR167 |
I | HOH2080 |
I | SER88 |
I | PHE89 |
I | THR90 |
I | ARG133 |
I | ARG135 |
I | SER164 |
I | SER165 |
I | ILE166 |
site_id | BC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 1244 |
Chain | Residue |
A | SER88 |
A | PHE89 |
A | THR90 |
A | ARG133 |
A | ARG135 |
A | SER165 |
A | ILE166 |
A | TYR167 |
A | HOH2070 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 1245 |
Chain | Residue |
A | PRO10 |
A | ILE11 |
A | TYR12 |
A | THR50 |
I | GLN108 |
I | LYS130 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 190 |
Details | DNA_BIND: H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00307 |
Chain | Residue | Details |
A | GLU37-SER56 | |
J | GLU37-SER56 | |
B | GLU37-SER56 | |
C | GLU37-SER56 | |
D | GLU37-SER56 | |
E | GLU37-SER56 | |
F | GLU37-SER56 | |
G | GLU37-SER56 | |
H | GLU37-SER56 | |
I | GLU37-SER56 |
site_id | SWS_FT_FI2 |
Number of Residues | 60 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25564531, ECO:0007744|PDB:4U0W |
Chain | Residue | Details |
A | PHE89 | |
B | SER165 | |
B | GLU222 | |
B | TYR228 | |
C | PHE89 | |
C | ARG133 | |
C | GLU145 | |
C | SER165 | |
C | GLU222 | |
C | TYR228 | |
D | PHE89 | |
A | ARG133 | |
D | ARG133 | |
D | GLU145 | |
D | SER165 | |
D | GLU222 | |
D | TYR228 | |
E | PHE89 | |
E | ARG133 | |
E | GLU145 | |
E | SER165 | |
E | GLU222 | |
A | GLU145 | |
E | TYR228 | |
F | PHE89 | |
F | ARG133 | |
F | GLU145 | |
F | SER165 | |
F | GLU222 | |
F | TYR228 | |
G | PHE89 | |
G | ARG133 | |
G | GLU145 | |
A | SER165 | |
G | SER165 | |
G | GLU222 | |
G | TYR228 | |
H | PHE89 | |
H | ARG133 | |
H | GLU145 | |
H | SER165 | |
H | GLU222 | |
H | TYR228 | |
I | PHE89 | |
A | GLU222 | |
I | ARG133 | |
I | GLU145 | |
I | SER165 | |
I | GLU222 | |
I | TYR228 | |
J | PHE89 | |
J | ARG133 | |
J | GLU145 | |
J | SER165 | |
J | GLU222 | |
A | TYR228 | |
J | TYR228 | |
B | PHE89 | |
B | ARG133 | |
B | GLU145 |