5JVL
C4-type pyruvate phospate dikinase: nucleotide binding domain with bound ATP analogue
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006090 | biological_process | pyruvate metabolic process |
A | 0009507 | cellular_component | chloroplast |
A | 0015979 | biological_process | photosynthesis |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
A | 0046872 | molecular_function | metal ion binding |
A | 0050242 | molecular_function | pyruvate, phosphate dikinase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006090 | biological_process | pyruvate metabolic process |
B | 0009507 | cellular_component | chloroplast |
B | 0015979 | biological_process | photosynthesis |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
B | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
B | 0046872 | molecular_function | metal ion binding |
B | 0050242 | molecular_function | pyruvate, phosphate dikinase activity |
C | 0003824 | molecular_function | catalytic activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006090 | biological_process | pyruvate metabolic process |
C | 0009507 | cellular_component | chloroplast |
C | 0015979 | biological_process | photosynthesis |
C | 0016301 | molecular_function | kinase activity |
C | 0016310 | biological_process | phosphorylation |
C | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
C | 0046872 | molecular_function | metal ion binding |
C | 0050242 | molecular_function | pyruvate, phosphate dikinase activity |
D | 0003824 | molecular_function | catalytic activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0006090 | biological_process | pyruvate metabolic process |
D | 0009507 | cellular_component | chloroplast |
D | 0015979 | biological_process | photosynthesis |
D | 0016301 | molecular_function | kinase activity |
D | 0016310 | biological_process | phosphorylation |
D | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
D | 0046872 | molecular_function | metal ion binding |
D | 0050242 | molecular_function | pyruvate, phosphate dikinase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue 6NQ A 901 |
Chain | Residue |
A | LYS25 |
A | LEU335 |
A | GLN336 |
A | ARG338 |
A | MG902 |
A | SER93 |
A | ARG95 |
A | THR108 |
A | SER242 |
A | MET243 |
A | VAL244 |
A | GLY279 |
A | GLU324 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue MG A 902 |
Chain | Residue |
A | GLU324 |
A | GLN336 |
A | 6NQ901 |
site_id | AC3 |
Number of Residues | 11 |
Details | binding site for residue PEP A 903 |
Chain | Residue |
A | ARG562 |
A | ARG619 |
A | MET746 |
A | GLU748 |
A | GLY769 |
A | THR770 |
A | ASN771 |
A | ASP772 |
A | ARG782 |
A | CYS834 |
A | MG904 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue MG A 904 |
Chain | Residue |
A | ARG619 |
A | ASP622 |
A | GLU748 |
A | ASP772 |
A | PEP903 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue PEP B 901 |
Chain | Residue |
B | ARG562 |
B | ARG619 |
B | GLU748 |
B | GLY769 |
B | THR770 |
B | ASN771 |
B | ASP772 |
B | CYS834 |
B | MG902 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue MG B 902 |
Chain | Residue |
B | GLU748 |
B | ASP772 |
B | PEP901 |
site_id | AC7 |
Number of Residues | 12 |
Details | binding site for residue 6NQ C 901 |
Chain | Residue |
C | LYS25 |
C | SER93 |
C | ARG95 |
C | THR108 |
C | SER242 |
C | VAL244 |
C | GLY279 |
C | GLU280 |
C | GLU324 |
C | LEU335 |
C | GLN336 |
C | MG902 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue MG C 902 |
Chain | Residue |
C | GLU324 |
C | GLN336 |
C | 6NQ901 |
site_id | AC9 |
Number of Residues | 12 |
Details | binding site for residue PEP C 903 |
Chain | Residue |
C | HIS456 |
C | LEU560 |
C | ARG562 |
C | ARG619 |
C | MET746 |
C | GLU748 |
C | GLY769 |
C | THR770 |
C | ASN771 |
C | ASP772 |
C | ARG782 |
C | MG904 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue MG C 904 |
Chain | Residue |
C | ARG619 |
C | GLU748 |
C | ASP772 |
C | PEP903 |
site_id | AD2 |
Number of Residues | 15 |
Details | binding site for residue 6NQ D 901 |
Chain | Residue |
D | LYS25 |
D | SER93 |
D | ARG95 |
D | THR108 |
D | LEU110 |
D | SER242 |
D | MET243 |
D | VAL244 |
D | GLY279 |
D | VAL283 |
D | GLU324 |
D | LEU335 |
D | GLN336 |
D | ARG338 |
D | MG902 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue MG D 902 |
Chain | Residue |
D | GLU324 |
D | GLN336 |
D | 6NQ901 |
site_id | AD4 |
Number of Residues | 12 |
Details | binding site for residue PEP D 903 |
Chain | Residue |
D | THR770 |
D | ASN771 |
D | ASP772 |
D | ARG782 |
D | CYS834 |
D | MG904 |
D | HIS456 |
D | ARG562 |
D | ARG619 |
D | MET746 |
D | GLU748 |
D | GLY769 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue MG D 904 |
Chain | Residue |
D | ARG619 |
D | GLU748 |
D | ASP772 |
D | PEP903 |
Functional Information from PROSITE/UniProt
site_id | PS00370 |
Number of Residues | 12 |
Details | PEP_ENZYMES_PHOS_SITE PEP-utilizing enzymes phosphorylation site signature. GGmTsHAAVVAR |
Chain | Residue | Details |
A | GLY451-ARG462 |
site_id | PS00742 |
Number of Residues | 19 |
Details | PEP_ENZYMES_2 PEP-utilizing enzymes signature 2. DfFSFGTNDLtQMTFGysR |
Chain | Residue | Details |
A | ASP764-ARG782 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000250|UniProtKB:P11155 |
Chain | Residue | Details |
A | HIS456 | |
B | HIS456 | |
C | HIS456 | |
D | HIS456 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P11155 |
Chain | Residue | Details |
A | CYS834 | |
B | CYS834 | |
C | CYS834 | |
D | CYS834 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P11155 |
Chain | Residue | Details |
B | ARG619 | |
B | GLU748 | |
B | GLY769 | |
B | THR770 | |
B | ASN771 | |
B | ASP772 | |
C | ARG562 | |
C | ARG619 | |
C | GLU748 | |
C | GLY769 | |
C | THR770 | |
C | ASN771 | |
C | ASP772 | |
D | ARG562 | |
D | ARG619 | |
D | GLU748 | |
D | GLY769 | |
D | THR770 | |
D | ASN771 | |
D | ASP772 | |
A | ARG562 | |
A | ARG619 | |
A | GLU748 | |
A | GLY769 | |
A | THR770 | |
A | ASN771 | |
A | ASP772 | |
B | ARG562 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine; by PDRP1 => ECO:0000250 |
Chain | Residue | Details |
A | THR454 | |
B | THR454 | |
C | THR454 | |
D | THR454 |