1MO1
CRYSTAL STRUCTURE AT 1.8 ANGSTROMS OF SELENO METHIONYLED CRH, THE BACILLUS SUBTILIS CATABOLITE REPRESSION CONTAINING PROTEIN CRH REVEALS AN UNEXPECTED SWAPPING DOMAIN AS AN UNTERTWINNED DIMER
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| B | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| C | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| D | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 480 |
| Chain | Residue |
| A | ARG17 |
| D | LYS11 |
| D | HOH537 |
| D | HOH538 |
| D | HOH574 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 C 481 |
| Chain | Residue |
| C | GLU7 |
| C | ARG9 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 482 |
| Chain | Residue |
| D | HOH556 |
| D | GLU7 |
| D | ARG9 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 483 |
| Chain | Residue |
| B | LYS11 |
| B | HOH541 |
| B | HOH543 |
| C | ARG17 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 484 |
| Chain | Residue |
| A | SER46 |
| A | ILE47 |
| A | MSE48 |
| A | HOH502 |
| A | HOH549 |
| D | SER46 |
| D | HOH589 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 485 |
| Chain | Residue |
| B | SER46 |
| B | HOH502 |
| B | HOH590 |
| B | HOH592 |
| C | SER46 |
| C | ILE47 |
| C | MSE48 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 486 |
| Chain | Residue |
| B | GLU7 |
| B | ARG9 |
| B | HOH552 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 487 |
| Chain | Residue |
| A | GLU7 |
| A | ARG9 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 488 |
| Chain | Residue |
| B | LYS37 |
| B | ASP38 |
| B | HOH513 |
| B | HOH557 |
| B | HOH588 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 489 |
| Chain | Residue |
| D | LYS37 |
| D | ASP38 |
| D | HOH517 |
| D | HOH581 |
| D | HOH587 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 471 |
| Chain | Residue |
| B | ALA16 |
| B | HOH583 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GOL A 472 |
| Chain | Residue |
| A | GLU36 |
| A | LYS37 |
| A | ASP38 |
| A | GLU60 |
| A | VAL61 |
| A | THR62 |
| A | HOH499 |
| A | HOH532 |
| A | HOH582 |
| B | LYS5 |
| B | THR30 |
| B | HOH519 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL C 473 |
| Chain | Residue |
| C | LYS37 |
| C | ASP38 |
| C | VAL61 |
| C | THR62 |
| C | HOH500 |
| C | HOH510 |
| C | HOH519 |
| D | LYS5 |
| D | THR30 |
| D | HOH518 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 474 |
| Chain | Residue |
| C | GLU60 |
| C | GLN82 |
| C | HOH581 |
| D | LYS5 |
| D | GLU7 |
| D | ARG9 |
| D | HOH572 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 475 |
| Chain | Residue |
| A | GLU60 |
| A | GLN82 |
| B | GLU7 |
| B | HOH561 |
| D | GLU72 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL D 476 |
| Chain | Residue |
| D | ALA16 |
| D | GOL479 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 477 |
| Chain | Residue |
| A | HOH578 |
| B | MSE1 |
| B | VAL2 |
| B | GLN3 |
| B | GLN66 |
| B | GLY67 |
| B | GLU68 |
| D | GLN71 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 478 |
| Chain | Residue |
| B | GLN71 |
| D | MSE1 |
| D | VAL2 |
| D | GLN3 |
| D | GLN66 |
| D | GLY67 |
| D | HOH532 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 479 |
| Chain | Residue |
| D | GOL476 |
| D | HOH541 |
| D | ALA16 |
| D | ARG17 |
| D | ALA20 |
Functional Information from PROSITE/UniProt
| site_id | PS00589 |
| Number of Residues | 16 |
| Details | PTS_HPR_SER PTS HPR domain serine phosphorylation site signature. GKkVNaKSIMGLMsLA |
| Chain | Residue | Details |
| B | GLY39-ALA54 | |
| A | GLY39-ALA54 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by HPrK/P","evidences":[{"source":"PROSITE-ProRule","id":"PRU00681","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16316990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16411239","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






