4GW0
Crystal structure of arginine kinase in complex with imino-L-ornithine, MgADP, and nitrate.
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 | 24 |
Details | BINDING SITE FOR RESIDUE ADP A 401 |
Chain | Residue |
A | SER122 |
A | HIS284 |
A | ARG309 |
A | THR311 |
A | ARG312 |
A | GLY313 |
A | GLU314 |
A | ASP324 |
A | MG402 |
A | NO3404 |
A | HOH504 |
A | ARG124 |
A | HOH506 |
A | HOH507 |
A | HOH526 |
A | HOH528 |
A | HOH556 |
A | ARG126 |
A | HIS185 |
A | TRP221 |
A | ARG229 |
A | ARG280 |
A | SER282 |
A | VAL283 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 402 |
Chain | Residue |
A | ADP401 |
A | NO3404 |
A | HOH504 |
A | HOH507 |
A | HOH618 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ILO A 403 |
Chain | Residue |
A | SER63 |
A | GLY64 |
A | VAL65 |
A | GLY66 |
A | TYR68 |
A | GLU225 |
A | CYS271 |
A | THR273 |
A | GLU314 |
A | HIS315 |
A | NO3404 |
A | HOH529 |
A | HOH536 |
A | HOH646 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE NO3 A 404 |
Chain | Residue |
A | ARG126 |
A | GLU225 |
A | ARG229 |
A | ASN274 |
A | ARG309 |
A | ADP401 |
A | MG402 |
A | ILO403 |
A | HOH504 |
Functional Information from PROSITE/UniProt
site_id | PS00112 |
Number of Residues | 7 |
Details | PHOSPHAGEN_KINASE Phosphagen kinase active site signature. CP.TNLGT |
Chain | Residue | Details |
A | CYS271-THR277 |
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 | CYS271 | |
A | ARG280 | |
A | ARG309 | |
A | GLU314 |
Catalytic Information from CSA
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 | CYS271 | 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 |