7E5W
The structure of CcpA from Staphylococcus aureus
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 |
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 |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 401 |
Chain | Residue |
A | VAL14 |
A | SER15 |
A | THR18 |
A | LYS30 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 402 |
Chain | Residue |
A | ARG10 |
A | SER15 |
A | MET16 |
A | LYS223 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 403 |
Chain | Residue |
A | ALA50 |
A | ARG300 |
A | ARG47 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 401 |
Chain | Residue |
B | ARG10 |
B | SER15 |
B | MET16 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 402 |
Chain | Residue |
B | LYS304 |
B | ILE311 |
B | GLU312 |
B | GLU313 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue SO4 C 401 |
Chain | Residue |
B | LYS223 |
C | ARG10 |
C | SER15 |
C | MET16 |
Functional Information from PROSITE/UniProt
site_id | PS00356 |
Number of Residues | 19 |
Details | HTH_LACI_1 LacI-type HTH domain signature. IyDVAreArVSmaTVsrVV |
Chain | Residue | Details |
A | ILE5-VAL23 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 57 |
Details | DNA_BIND: H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00111 |
Chain | Residue | Details |
A | ILE5-ASN24 | |
B | ILE5-ASN24 | |
C | ILE5-ASN24 |