4BG4
Crystal structure of Litopenaeus vannamei arginine kinase in a ternary analog complex with arginine, ADP-Mg and NO3
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 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 | 0034618 | molecular_function | arginine binding |
| A | 0046072 | biological_process | dTDP metabolic process |
| A | 0046314 | biological_process | phosphocreatine biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004054 | molecular_function | arginine kinase activity |
| B | 0004111 | molecular_function | creatine 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 | 0034618 | molecular_function | arginine binding |
| B | 0046072 | biological_process | dTDP metabolic process |
| B | 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 400 |
| Chain | Residue |
| A | SER122 |
| A | VAL283 |
| A | HIS284 |
| A | ARG309 |
| A | THR311 |
| A | ARG312 |
| A | GLY313 |
| A | GLU314 |
| A | ASP324 |
| A | NO3405 |
| A | MG406 |
| A | ARG124 |
| A | HOH2167 |
| A | HOH2233 |
| A | HOH2242 |
| A | HOH2297 |
| A | HOH2330 |
| A | ARG126 |
| A | HIS185 |
| A | TRP221 |
| A | ARG229 |
| A | MET233 |
| A | ARG280 |
| A | SER282 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ARG A 403 |
| Chain | Residue |
| A | SER63 |
| A | GLY64 |
| A | VAL65 |
| A | GLY66 |
| A | TYR68 |
| A | GLU225 |
| A | CYS271 |
| A | GLU314 |
| A | NO3405 |
| A | HOH2077 |
| A | HOH2091 |
| A | HOH2316 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE NO3 A 405 |
| Chain | Residue |
| A | ARG126 |
| A | GLU225 |
| A | ARG229 |
| A | ASN274 |
| A | ARG309 |
| A | GLU314 |
| A | ADP400 |
| A | ARG403 |
| A | MG406 |
| A | HOH2295 |
| A | HOH2314 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 406 |
| Chain | Residue |
| A | ADP400 |
| A | NO3405 |
| A | HOH2272 |
| A | HOH2273 |
| A | HOH2314 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME A 409 |
| Chain | Residue |
| A | LEU46 |
| A | ASP52 |
| A | PRO138 |
| A | CYS139 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ADP B 400 |
| Chain | Residue |
| B | SER122 |
| B | ARG124 |
| B | ARG126 |
| B | HIS185 |
| B | TRP221 |
| B | ARG229 |
| B | MET233 |
| B | ARG280 |
| B | SER282 |
| B | VAL283 |
| B | HIS284 |
| B | ARG309 |
| B | THR311 |
| B | ARG312 |
| B | GLY313 |
| B | GLU314 |
| B | ASP324 |
| B | NO3405 |
| B | MG407 |
| B | HOH2179 |
| B | HOH2185 |
| B | HOH2210 |
| B | HOH2213 |
| B | HOH2254 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ARG B 403 |
| Chain | Residue |
| B | SER63 |
| B | GLY64 |
| B | VAL65 |
| B | GLY66 |
| B | TYR68 |
| B | GLU225 |
| B | CYS271 |
| B | THR273 |
| B | GLU314 |
| B | NO3405 |
| B | HOH2062 |
| B | HOH2076 |
| B | HOH2247 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE NO3 B 405 |
| Chain | Residue |
| B | ADP400 |
| B | ARG403 |
| B | MG407 |
| B | HOH2228 |
| B | ARG126 |
| B | GLU225 |
| B | ARG229 |
| B | ASN274 |
| B | ARG309 |
| B | GLU314 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME B 406 |
| Chain | Residue |
| B | ASP52 |
| B | CYS139 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 407 |
| Chain | Residue |
| B | ADP400 |
| B | NO3405 |
| B | HOH2210 |
| B | HOH2211 |
| B | HOH2245 |
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 |
| B | CYS271-THR277 | |
| A | CYS271-THR277 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 164 |
| Details | Domain: {"description":"Phosphagen kinase N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00842","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23873077","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BG4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BHL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00843","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23873077","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BG4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23873077","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BG4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
