4QPJ
2.7 Angstrom Structure of a Phosphotransferase in Complex with a Receiver Domain
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000160 | biological_process | phosphorelay signal transduction system |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0018197 | biological_process | peptidyl-aspartic acid modification |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0000160 | biological_process | phosphorelay signal transduction system |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| B | 0018197 | biological_process | peptidyl-aspartic acid modification |
| B | 0042803 | molecular_function | protein homodimerization activity |
| C | 0000160 | biological_process | phosphorelay signal transduction system |
| D | 0000160 | biological_process | phosphorelay signal transduction system |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 301 |
| Chain | Residue |
| A | ASP23 |
| A | ARG61 |
| A | ALA65 |
| A | PHE69 |
| A | TYR91 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 302 |
| Chain | Residue |
| A | ARG19 |
| A | LEU121 |
| A | HIS177 |
| A | GLN180 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 303 |
| Chain | Residue |
| A | LYS96 |
| A | PRO97 |
| A | ASN124 |
| A | ILE127 |
| A | HOH413 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 304 |
| Chain | Residue |
| A | PHE92 |
| A | ARG93 |
| A | GLU95 |
| A | PRO97 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 301 |
| Chain | Residue |
| B | ILE20 |
| B | ASP23 |
| B | ARG61 |
| B | PHE64 |
| B | ALA65 |
| B | PHE69 |
| B | TYR91 |
| B | LEU121 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 302 |
| Chain | Residue |
| B | SER26 |
| B | ALA30 |
| B | ASN33 |
| D | SER15 |
| D | LYS101 |
| D | PRO102 |
| D | PHE103 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 303 |
| Chain | Residue |
| B | ARG19 |
| B | GLN180 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA B 304 |
| Chain | Residue |
| B | PHE92 |
| B | GLU95 |
| B | PRO97 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 201 |
| Chain | Residue |
| A | GLN78 |
| A | LEU107 |
| A | LEU108 |
| A | PRO109 |
| A | ASP141 |
| C | ARG64 |
| C | PHE93 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA C 202 |
| Chain | Residue |
| C | TYR43 |
| C | ASP44 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 201 |
| Chain | Residue |
| D | GLU7 |
| D | ASP8 |
| D | ASP9 |
| D | ASP51 |
| D | ASN53 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000305|PubMed:26124143 |
| Chain | Residue | Details |
| C | ASP51 | |
| D | ASP51 |
