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 |