6FH1
Protein arginine kinase McsB in the apo state
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004111 | molecular_function | creatine kinase activity |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005615 | cellular_component | extracellular space |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| A | 0016775 | molecular_function | phosphotransferase activity, nitrogenous group as acceptor |
| A | 0046314 | biological_process | phosphocreatine biosynthetic process |
| A | 1990424 | molecular_function | protein arginine kinase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004111 | molecular_function | creatine kinase activity |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005615 | cellular_component | extracellular space |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| B | 0016775 | molecular_function | phosphotransferase activity, nitrogenous group as acceptor |
| B | 0046314 | biological_process | phosphocreatine biosynthetic process |
| B | 1990424 | molecular_function | protein arginine kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue FMT A 401 |
| Chain | Residue |
| A | SER27 |
| A | ARG29 |
| A | SER179 |
| A | MET181 |
| A | HOH535 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue FMT A 402 |
| Chain | Residue |
| A | GLU122 |
| A | CYS168 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | GLU122 |
| A | ARG126 |
| A | ARG177 |
| A | HOH502 |
| A | HOH507 |
| A | ARG29 |
| A | ARG31 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | THR9 |
| A | ALA10 |
| A | VAL11 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | LYS270 |
| A | SER274 |
| A | ILE277 |
| A | CYS292 |
| A | HOH539 |
| A | HOH546 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | ALA50 |
| A | PRO103 |
| A | PHE104 |
| A | GLY105 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | SER144 |
| A | ASP147 |
| A | GLU234 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 408 |
| Chain | Residue |
| A | VAL89 |
| A | GLU90 |
| A | HIS92 |
| A | TYR211 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 409 |
| Chain | Residue |
| A | ARG208 |
| A | GLY209 |
| A | THR210 |
| A | TYR211 |
| A | GLY212 |
| A | GLY214 |
| A | GLU216 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 410 |
| Chain | Residue |
| A | VAL11 |
| A | SER12 |
| A | MET15 |
| A | LEU93 |
| A | GLU113 |
| A | HOH581 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 411 |
| Chain | Residue |
| A | ALA258 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 412 |
| Chain | Residue |
| A | VAL11 |
| A | SER16 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 413 |
| Chain | Residue |
| A | GLN17 |
| A | GLN135 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 414 |
| Chain | Residue |
| A | HIS92 |
| A | MET181 |
| A | TYR211 |
| A | ASN314 |
| A | ILE318 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 415 |
| Chain | Residue |
| A | TYR66 |
| A | GLY67 |
| A | GLU68 |
| A | ALA69 |
| A | HOH515 |
| A | HOH660 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 416 |
| Chain | Residue |
| A | HOH514 |
| A | HOH601 |
| A | HOH627 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 417 |
| Chain | Residue |
| A | ALA137 |
| A | LEU140 |
| A | GLU141 |
| A | HOH503 |
| A | HOH573 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue IMD A 418 |
| Chain | Residue |
| A | GLU151 |
| A | TYR164 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 401 |
| Chain | Residue |
| B | SER286 |
| B | MET317 |
| B | THR320 |
| B | GLN321 |
| B | HOH570 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | HIS92 |
| B | TYR211 |
| B | ASN314 |
| site_id | AE3 |
| Number of Residues | 5 |
| Details | binding site for residue IMD B 403 |
| Chain | Residue |
| B | SER27 |
| B | ARG29 |
| B | LEU130 |
| B | SER179 |
| B | MET181 |
| site_id | AE4 |
| Number of Residues | 2 |
| Details | binding site for residue IMD B 404 |
| Chain | Residue |
| B | LEU319 |
| B | PHE324 |
| site_id | AE5 |
| Number of Residues | 2 |
| Details | binding site for residue IMD B 405 |
| Chain | Residue |
| B | SER144 |
| B | ASP147 |
Functional Information from PROSITE/UniProt
| site_id | PS00112 |
| Number of Residues | 7 |
| Details | PHOSPHAGEN_KINASE Phosphagen kinase active site signature. CP.TNVGT |
| Chain | Residue | Details |
| A | CYS168-THR174 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 231 |
| Details | Domain: {"description":"Phosphagen kinase C-terminal"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Motif: {"description":"RDXXRA motif of the pArg binding pocket involved in allosteric regulation","evidences":[{"source":"PubMed","id":"30962626","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30962626","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00602","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00602","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"30962626","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
