1SD0
Structure of arginine kinase C271A mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004054 | molecular_function | arginine kinase activity |
| A | 0004111 | molecular_function | creatine 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 | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| A | 0046314 | biological_process | phosphocreatine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE NO3 A 401 |
| Chain | Residue |
| A | ARG126 |
| A | HOH417 |
| A | GLU225 |
| A | ARG229 |
| A | ASN274 |
| A | ARG309 |
| A | GLU314 |
| A | ADP400 |
| A | MG402 |
| A | ARG403 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 402 |
| Chain | Residue |
| A | ADP400 |
| A | NO3401 |
| A | HOH417 |
| A | HOH431 |
| A | HOH432 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 404 |
| Chain | Residue |
| A | ALA271 |
| A | PRO272 |
| A | THR273 |
| A | ARG403 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ARG A 403 |
| Chain | Residue |
| A | SER63 |
| A | GLY64 |
| A | VAL65 |
| A | GLY66 |
| A | TYR68 |
| A | GLU225 |
| A | ALA271 |
| A | THR273 |
| A | GLU314 |
| A | HIS315 |
| A | NO3401 |
| A | CL404 |
| A | HOH438 |
| A | HOH467 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ADP A 400 |
| Chain | Residue |
| A | SER122 |
| A | ARG124 |
| A | ARG126 |
| A | HIS185 |
| A | TRP221 |
| A | ARG229 |
| A | ARG280 |
| A | SER282 |
| A | VAL283 |
| A | HIS284 |
| A | ARG309 |
| A | THR311 |
| A | ARG312 |
| A | GLY313 |
| A | GLU314 |
| A | ASP324 |
| A | NO3401 |
| A | MG402 |
| A | HOH409 |
| A | HOH412 |
| A | HOH417 |
| A | HOH426 |
| A | HOH431 |
| A | HOH449 |
| A | HOH456 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY64 | |
| A | SER122 | |
| A | HIS185 | |
| A | GLU225 | |
| A | ARG229 | |
| A | ALA271 | |
| A | ARG280 | |
| A | ARG309 | |
| A | GLU314 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1bg0 |
| Chain | Residue | Details |
| A | ARG309 | |
| A | ARG280 | |
| A | ARG229 | |
| A | ARG126 | |
| A | GLU225 |
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 86 |
| Chain | Residue | Details |
| A | ARG126 | electrostatic stabiliser, hydrogen bond donor |
| A | GLU225 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ARG229 | electrostatic stabiliser, hydrogen bond donor |
| A | ALA271 | electrostatic stabiliser, hydrogen bond acceptor, steric role |
| A | THR273 | electrostatic stabiliser, hydrogen bond donor |
| A | ARG280 | electrostatic stabiliser, hydrogen bond donor |
| A | ARG309 | electrostatic stabiliser, hydrogen bond donor |
| A | GLU314 | electrostatic stabiliser |
