3Q15
Crystal Structure of RapH complexed with Spo0F
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0030420 | biological_process | establishment of competence for transformation |
| A | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| B | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0030420 | biological_process | establishment of competence for transformation |
| B | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| C | 0000160 | biological_process | phosphorelay signal transduction system |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016301 | molecular_function | kinase activity |
| C | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000160 | biological_process | phosphorelay signal transduction system |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016301 | molecular_function | kinase activity |
| D | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 377 |
| Chain | Residue |
| A | LYS153 |
| A | GLN154 |
| A | THR155 |
| A | PHE193 |
| A | LEU368 |
| A | GLU371 |
| A | HOH453 |
| A | HOH466 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 378 |
| Chain | Residue |
| A | ARG178 |
| A | LYS144 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 377 |
| Chain | Residue |
| B | LYS153 |
| B | GLN154 |
| B | THR155 |
| B | LEU368 |
| B | GLU371 |
| B | HOH389 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 B 378 |
| Chain | Residue |
| B | ARG178 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 125 |
| Chain | Residue |
| C | ASP11 |
| C | ASP54 |
| C | LYS56 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG D 125 |
| Chain | Residue |
| D | ASP11 |
| D | ASP54 |
| D | LYS56 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| C | ASP10 | |
| C | ASP11 | |
| C | ASP54 | |
| C | LYS56 | |
| D | ASP10 | |
| D | ASP11 | |
| D | ASP54 | |
| D | LYS56 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:9254596 |
| Chain | Residue | Details |
| C | ASP54 | |
| D | ASP54 |
