3TLX
Crystal Structure of PF10_0086, adenylate kinase from plasmodium falciparum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004017 | molecular_function | AMP kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006091 | biological_process | generation of precursor metabolites and energy |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
| A | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004017 | molecular_function | AMP kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0006091 | biological_process | generation of precursor metabolites and energy |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
| B | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| B | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004017 | molecular_function | AMP kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005829 | cellular_component | cytosol |
| C | 0006091 | biological_process | generation of precursor metabolites and energy |
| C | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
| C | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| C | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004017 | molecular_function | AMP kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005829 | cellular_component | cytosol |
| D | 0006091 | biological_process | generation of precursor metabolites and energy |
| D | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
| D | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| D | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ADP B 243 |
| Chain | Residue |
| B | PRO37 |
| B | ILE164 |
| B | TYR165 |
| B | HIS166 |
| B | PHE169 |
| B | GLN227 |
| B | PRO228 |
| B | ALA229 |
| B | ADP244 |
| B | GLY38 |
| B | SER39 |
| B | GLY40 |
| B | LYS41 |
| B | GLY42 |
| B | THR43 |
| B | ARG151 |
| B | ARG155 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 243 |
| Chain | Residue |
| A | GLN187 |
| A | ARG188 |
| A | GLU189 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 244 |
| Chain | Residue |
| A | HIS239 |
| A | GLY242 |
| B | GLN132 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ATP D 243 |
| Chain | Residue |
| D | GLY42 |
| D | THR43 |
| D | ARG151 |
| D | ARG155 |
| D | GLN227 |
| D | PRO228 |
| D | ALA229 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADP B 244 |
| Chain | Residue |
| B | PRO37 |
| B | SER58 |
| B | THR59 |
| B | GLY60 |
| B | LEU63 |
| B | ARG64 |
| B | ILE81 |
| B | LYS85 |
| B | LEU86 |
| B | VAL87 |
| B | ASP112 |
| B | GLY113 |
| B | TYR114 |
| B | ARG116 |
| B | GLN120 |
| B | ARG155 |
| B | ARG188 |
| B | ASP190 |
| B | ARG199 |
| B | ADP243 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AMP A 245 |
| Chain | Residue |
| A | THR59 |
| A | GLY60 |
| A | LEU63 |
| A | ILE81 |
| A | LYS85 |
| A | LEU86 |
| A | VAL87 |
| A | VAL92 |
| A | GLY113 |
| A | TYR114 |
| A | GLN120 |
| A | ARG199 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADP A 246 |
| Chain | Residue |
| A | ALA36 |
| A | GLY38 |
| A | SER39 |
| A | GLY40 |
| A | LYS41 |
| A | GLY42 |
| A | THR43 |
| A | ARG151 |
| A | ARG155 |
| A | ILE164 |
| A | TYR165 |
| A | HIS166 |
| A | PHE169 |
| A | GLN227 |
| A | ALA229 |
Functional Information from PROSITE/UniProt
| site_id | PS00113 |
| Number of Residues | 12 |
| Details | ADENYLATE_KINASE Adenylate kinase signature. FILDGYPRnvkQ |
| Chain | Residue | Details |
| A | PHE109-GLN120 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 58 |
| Details | Region: {"description":"NMP","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2011","submissionDatabase":"PDB data bank","title":"Crystal Structure of PF10_0086, adenylate kinase from plasmodium falciparum.","authors":["Wernimont A.K.","Loppnau P.","Crombet L.","Weadge J.","Perieteanu A.","Edwards A.M.","Arrowsmith C.H.","Park H.","Bountra C.","Hui R.","Amani M."]}},{"source":"PDB","id":"3TLX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 74 |
| Details | Region: {"description":"LID","evidences":[{"source":"UniProtKB","id":"P00568","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 60 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2011","submissionDatabase":"PDB data bank","title":"Crystal Structure of PF10_0086, adenylate kinase from plasmodium falciparum.","authors":["Wernimont A.K.","Loppnau P.","Crombet L.","Weadge J.","Perieteanu A.","Edwards A.M.","Arrowsmith C.H.","Park H.","Bountra C.","Hui R.","Amani M."]}},{"source":"PDB","id":"3TLX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
