5Z7H
Crystal structure of CcpE regulatory domain in citrate-bound form from Staphyloccocus aureus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000976 | molecular_function | transcription cis-regulatory region 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 | 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 | 0003700 | molecular_function | DNA-binding transcription factor activity |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0000976 | molecular_function | transcription cis-regulatory region binding |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0000976 | molecular_function | transcription cis-regulatory region binding |
| E | 0003700 | molecular_function | DNA-binding transcription factor activity |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
| F | 0000976 | molecular_function | transcription cis-regulatory region binding |
| F | 0003700 | molecular_function | DNA-binding transcription factor activity |
| F | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue FLC A 301 |
| Chain | Residue |
| A | SER98 |
| A | VAL213 |
| A | ARG256 |
| A | HOH402 |
| A | HOH406 |
| A | HOH414 |
| A | HOH443 |
| A | HOH481 |
| A | HOH486 |
| A | HOH511 |
| A | SER99 |
| A | LEU100 |
| A | SER128 |
| A | THR129 |
| A | GLU130 |
| A | ARG145 |
| A | ASP211 |
| A | GLN212 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue FLC B 301 |
| Chain | Residue |
| B | SER98 |
| B | THR129 |
| B | ARG145 |
| B | GLN183 |
| B | ALA184 |
| B | ASP211 |
| B | GLN212 |
| B | VAL213 |
| B | ARG256 |
| B | HOH402 |
| B | HOH430 |
| B | HOH461 |
| B | HOH464 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | binding site for residue FLC C 301 |
| Chain | Residue |
| C | SER98 |
| C | SER99 |
| C | LEU100 |
| C | SER128 |
| C | THR129 |
| C | ARG145 |
| C | GLN183 |
| C | ASP211 |
| C | GLN212 |
| C | VAL213 |
| C | ARG256 |
| C | HOH403 |
| C | HOH421 |
| C | HOH428 |
| C | HOH447 |
| C | HOH456 |
| C | HOH479 |
| C | HOH480 |
| C | HOH495 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue FLC D 301 |
| Chain | Residue |
| D | SER98 |
| D | LEU100 |
| D | SER128 |
| D | THR129 |
| D | ARG145 |
| D | GLN183 |
| D | ALA184 |
| D | VAL213 |
| D | ARG256 |
| D | HOH402 |
| D | HOH406 |
| D | HOH423 |
| D | HOH474 |
| D | HOH503 |
| D | HOH549 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | binding site for residue FLC E 301 |
| Chain | Residue |
| E | SER98 |
| E | SER99 |
| E | LEU100 |
| E | THR129 |
| E | ARG145 |
| E | GLN183 |
| E | ALA184 |
| E | ASP211 |
| E | GLN212 |
| E | VAL213 |
| E | ARG256 |
| E | HOH404 |
| E | HOH417 |
| E | HOH420 |
| E | HOH431 |
| E | HOH447 |
| E | HOH488 |
| site_id | AC6 |
| Number of Residues | 20 |
| Details | binding site for residue FLC F 301 |
| Chain | Residue |
| F | HOH464 |
| F | HOH485 |
| F | HOH492 |
| F | SER98 |
| F | SER99 |
| F | LEU100 |
| F | SER128 |
| F | THR129 |
| F | GLU130 |
| F | ARG145 |
| F | ALA184 |
| F | ASP211 |
| F | GLN212 |
| F | VAL213 |
| F | ARG256 |
| F | HOH404 |
| F | HOH407 |
| F | HOH423 |
| F | HOH425 |
| F | HOH431 |
