6IS1
Crystal Structure of Staphylococcus aureus response regulator ArlR receiver domain in complex with BeF3 and Mg
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000160 | biological_process | phosphorelay signal transduction system |
| A | 0000976 | molecular_function | transcription cis-regulatory region binding |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0000160 | biological_process | phosphorelay signal transduction system |
| B | 0000976 | molecular_function | transcription cis-regulatory region binding |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0000160 | biological_process | phosphorelay signal transduction system |
| C | 0000976 | molecular_function | transcription cis-regulatory region binding |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0000160 | biological_process | phosphorelay signal transduction system |
| D | 0000976 | molecular_function | transcription cis-regulatory region binding |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0000160 | biological_process | phosphorelay signal transduction system |
| E | 0000976 | molecular_function | transcription cis-regulatory region binding |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
| F | 0000160 | biological_process | phosphorelay signal transduction system |
| F | 0000976 | molecular_function | transcription cis-regulatory region binding |
| F | 0006355 | biological_process | regulation of DNA-templated transcription |
| G | 0000160 | biological_process | phosphorelay signal transduction system |
| G | 0000976 | molecular_function | transcription cis-regulatory region binding |
| G | 0006355 | biological_process | regulation of DNA-templated transcription |
| H | 0000160 | biological_process | phosphorelay signal transduction system |
| H | 0000976 | molecular_function | transcription cis-regulatory region binding |
| H | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue BEF A 301 |
| Chain | Residue |
| A | ASP52 |
| A | HOH554 |
| A | HOH567 |
| A | LEU53 |
| A | MET54 |
| A | THR79 |
| A | ALA80 |
| A | LYS101 |
| A | MG302 |
| A | HOH439 |
| A | HOH501 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | ASP9 |
| A | ASP52 |
| A | MET54 |
| A | BEF301 |
| A | HOH439 |
| A | HOH501 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue BEF C 301 |
| Chain | Residue |
| C | ASP52 |
| C | LEU53 |
| C | MET54 |
| C | THR79 |
| C | ALA80 |
| C | LYS101 |
| C | MG302 |
| C | HOH402 |
| C | HOH431 |
| C | HOH478 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 302 |
| Chain | Residue |
| C | ASP9 |
| C | ASP52 |
| C | MET54 |
| C | BEF301 |
| C | HOH402 |
| C | HOH431 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residue BEF B 301 |
| Chain | Residue |
| B | ASP52 |
| B | LEU53 |
| B | MET54 |
| B | THR79 |
| B | ALA80 |
| B | LYS101 |
| B | MG302 |
| B | HOH435 |
| B | HOH511 |
| B | HOH555 |
| B | HOH575 |
| B | HOH591 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 302 |
| Chain | Residue |
| B | ASP9 |
| B | ASP52 |
| B | MET54 |
| B | BEF301 |
| B | HOH435 |
| B | HOH511 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue IMD B 303 |
| Chain | Residue |
| B | ASP96 |
| B | HOH408 |
| D | ASP96 |
| D | HOH423 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | binding site for residue BEF D 301 |
| Chain | Residue |
| D | ASP52 |
| D | LEU53 |
| D | MET54 |
| D | THR79 |
| D | ALA80 |
| D | LYS101 |
| D | MG302 |
| D | HOH421 |
| D | HOH476 |
| D | HOH507 |
| G | HOH498 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 302 |
| Chain | Residue |
| D | ASP9 |
| D | ASP52 |
| D | MET54 |
| D | BEF301 |
| D | HOH421 |
| D | HOH476 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue BEF E 301 |
| Chain | Residue |
| E | ASP52 |
| E | LEU53 |
| E | MET54 |
| E | THR79 |
| E | ALA80 |
| E | LYS101 |
| E | MG302 |
| E | HOH405 |
| E | HOH406 |
| E | HOH471 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue MG E 302 |
| Chain | Residue |
| E | GLU8 |
| E | ASP9 |
| E | ASP52 |
| E | MET54 |
| E | BEF301 |
| E | HOH405 |
| E | HOH406 |
| site_id | AD3 |
| Number of Residues | 10 |
| Details | binding site for residue BEF F 301 |
| Chain | Residue |
| F | ASP52 |
| F | LEU53 |
| F | MET54 |
| F | THR79 |
| F | ALA80 |
| F | LYS101 |
| F | MG302 |
| F | HOH413 |
| F | HOH511 |
| F | HOH565 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue MG F 302 |
| Chain | Residue |
| F | ASP9 |
| F | ASP52 |
| F | MET54 |
| F | BEF301 |
| F | HOH413 |
| F | HOH511 |
| site_id | AD5 |
| Number of Residues | 9 |
| Details | binding site for residue IMD F 303 |
| Chain | Residue |
| E | ASP96 |
| E | ASP97 |
| E | ILE115 |
| F | ASP96 |
| F | ASP97 |
| F | ILE115 |
| F | HOH409 |
| F | HOH416 |
| F | HOH458 |
| site_id | AD6 |
| Number of Residues | 9 |
| Details | binding site for residue BEF G 301 |
| Chain | Residue |
| G | ASP52 |
| G | LEU53 |
| G | MET54 |
| G | THR79 |
| G | ALA80 |
| G | LYS101 |
| G | MG302 |
| G | HOH441 |
| G | HOH497 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue MG G 302 |
| Chain | Residue |
| G | ASP9 |
| G | ASP52 |
| G | MET54 |
| G | BEF301 |
| G | HOH441 |
| site_id | AD8 |
| Number of Residues | 11 |
| Details | binding site for residue BEF H 301 |
| Chain | Residue |
| H | ASP52 |
| H | LEU53 |
| H | MET54 |
| H | THR79 |
| H | ALA80 |
| H | LYS101 |
| H | MG302 |
| H | HOH414 |
| H | HOH495 |
| H | HOH551 |
| H | HOH567 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue MG H 302 |
| Chain | Residue |
| H | ASP9 |
| H | ASP52 |
| H | MET54 |
| H | BEF301 |
| H | HOH414 |
| H | HOH495 |
| site_id | AE1 |
| Number of Residues | 10 |
| Details | binding site for residue IMD H 303 |
| Chain | Residue |
| G | ASP96 |
| G | ASP97 |
| G | ILE115 |
| G | HOH428 |
| H | ASP96 |
| H | ASP97 |
| H | ILE115 |
| H | HOH407 |
| H | HOH425 |
| H | HOH448 |
Functional Information from PROSITE/UniProt
| site_id | PS00217 |
| Number of Residues | 26 |
| Details | SUGAR_TRANSPORT_2 Sugar transport proteins signature 2. VaGLDyGAddyivkpFdiEellariR |
| Chain | Residue | Details |
| A | VAL88-ARG113 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 904 |
| Details | Domain: {"description":"Response regulatory","evidences":[{"source":"PROSITE-ProRule","id":"PRU00169","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"4-aspartylphosphate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00169","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






