4JYK
Structure of E. coli Transcriptional Regulator RutR with bound uracil
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 | 0005515 | molecular_function | protein binding |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
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 | 0005515 | molecular_function | protein binding |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0045892 | biological_process | negative regulation of DNA-templated transcription |
B | 0045893 | biological_process | positive regulation of DNA-templated transcription |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 301 |
Chain | Residue |
A | ARG85 |
A | GLU86 |
A | ASP87 |
B | LYS19 |
B | ASN54 |
B | TYR58 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 302 |
Chain | Residue |
A | ALA92 |
A | HOH431 |
A | ALA89 |
A | PRO90 |
A | LEU91 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 303 |
Chain | Residue |
A | LYS95 |
A | ARG99 |
A | GLN202 |
A | HOH446 |
A | HOH448 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 304 |
Chain | Residue |
A | ARG12 |
A | SER13 |
A | VAL16 |
A | HOH470 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE URA A 305 |
Chain | Residue |
A | LEU74 |
A | TRP77 |
A | LYS101 |
A | PHE115 |
A | TRP167 |
A | GLN171 |
A | HOH404 |
B | PHE176 |
B | GLN179 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 301 |
Chain | Residue |
B | ARG40 |
B | LEU41 |
B | GLU42 |
B | LYS52 |
B | HOH537 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 302 |
Chain | Residue |
A | ARG85 |
B | SER51 |
B | ASN54 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 303 |
Chain | Residue |
B | LYS95 |
B | ARG99 |
B | GLN202 |
B | HOH420 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE URA B 304 |
Chain | Residue |
A | PHE176 |
A | GLN179 |
B | LEU74 |
B | TRP77 |
B | LYS101 |
B | PHE115 |
B | TRP167 |
B | GLN171 |
B | HOH408 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 38 |
Details | DNA_BIND: H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00335 |
Chain | Residue | Details |
A | THR39-TYR58 | |
B | THR39-TYR58 |