2XDF
Solution Structure of the Enzyme I Dimer Complexed with HPr Using Residual Dipolar Couplings and Small Angle X-Ray Scattering
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0008965 | molecular_function | phosphoenolpyruvate-protein phosphotransferase activity |
A | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
A | 0016301 | molecular_function | kinase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0008965 | molecular_function | phosphoenolpyruvate-protein phosphotransferase activity |
B | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
B | 0016301 | molecular_function | kinase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
C | 0004857 | molecular_function | enzyme inhibitor activity |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0008047 | molecular_function | enzyme activator activity |
C | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
C | 0016775 | molecular_function | phosphotransferase activity, nitrogenous group as acceptor |
C | 0030234 | molecular_function | enzyme regulator activity |
C | 0043609 | biological_process | regulation of carbon utilization |
C | 0045152 | molecular_function | antisigma factor binding |
C | 0045819 | biological_process | positive regulation of glycogen catabolic process |
D | 0004857 | molecular_function | enzyme inhibitor activity |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0008047 | molecular_function | enzyme activator activity |
D | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
D | 0016775 | molecular_function | phosphotransferase activity, nitrogenous group as acceptor |
D | 0030234 | molecular_function | enzyme regulator activity |
D | 0043609 | biological_process | regulation of carbon utilization |
D | 0045152 | molecular_function | antisigma factor binding |
D | 0045819 | biological_process | positive regulation of glycogen catabolic process |
Functional Information from PROSITE/UniProt
site_id | PS00369 |
Number of Residues | 8 |
Details | PTS_HPR_HIS PTS HPR domain histidine phosphorylation site signature. GLHTRPAA |
Chain | Residue | Details |
C | GLY613-ALA620 |
site_id | PS00370 |
Number of Residues | 12 |
Details | PEP_ENZYMES_PHOS_SITE PEP-utilizing enzymes phosphorylation site signature. GGrTsHTSIMAR |
Chain | Residue | Details |
A | GLY184-ARG195 |
site_id | PS00589 |
Number of Residues | 16 |
Details | PTS_HPR_SER PTS HPR domain serine phosphorylation site signature. GKsASaKSLFKLQtLG |
Chain | Residue | Details |
C | GLY639-GLY654 |
site_id | PS00742 |
Number of Residues | 19 |
Details | PEP_ENZYMES_2 PEP-utilizing enzymes signature 2. DfFSIGTNDLtQYTLAvdR |
Chain | Residue | Details |
A | ASP447-ARG465 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Pros-phosphohistidine intermediate => ECO:0000255|PROSITE-ProRule:PRU00681, ECO:0000269|PubMed:2261470 |
Chain | Residue | Details |
C | HIS615 | |
D | HIS615 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:12705838, ECO:0000305|PubMed:17053069 |
Chain | Residue | Details |
A | CYS502 | |
B | CYS502 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P23533 |
Chain | Residue | Details |
A | ARG296 | |
A | ARG465 | |
B | ARG296 | |
B | ARG465 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17053069 |
Chain | Residue | Details |
A | ARG332 | |
A | GLU431 | |
A | ASN454 | |
A | ASP455 | |
B | ARG332 | |
B | GLU431 | |
B | ASN454 | |
B | ASP455 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 920 |
Chain | Residue | Details |
A | HIS189 | covalent catalysis |
A | GLU431 | metal ligand |
A | ASP455 | metal ligand |
A | CYS502 | proton shuttle (general acid/base) |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 920 |
Chain | Residue | Details |
B | HIS189 | covalent catalysis |
B | GLU431 | metal ligand |
B | ASP455 | metal ligand |
B | CYS502 | proton shuttle (general acid/base) |