3EPS
The crystal structure of isocitrate dehydrogenase kinase/phosphatase from E. coli
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0004721 | molecular_function | phosphoprotein phosphatase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006006 | biological_process | glucose metabolic process |
A | 0006097 | biological_process | glyoxylate cycle |
A | 0006099 | biological_process | tricarboxylic acid cycle |
A | 0006470 | biological_process | protein dephosphorylation |
A | 0008772 | molecular_function | [isocitrate dehydrogenase (NADP+)] kinase activity |
A | 0016208 | molecular_function | AMP binding |
A | 0016310 | biological_process | phosphorylation |
A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
A | 0016791 | molecular_function | phosphatase activity |
A | 0018105 | biological_process | peptidyl-serine phosphorylation |
A | 0050790 | biological_process | regulation of catalytic activity |
B | 0004674 | molecular_function | protein serine/threonine kinase activity |
B | 0004721 | molecular_function | phosphoprotein phosphatase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006006 | biological_process | glucose metabolic process |
B | 0006097 | biological_process | glyoxylate cycle |
B | 0006099 | biological_process | tricarboxylic acid cycle |
B | 0006470 | biological_process | protein dephosphorylation |
B | 0008772 | molecular_function | [isocitrate dehydrogenase (NADP+)] kinase activity |
B | 0016208 | molecular_function | AMP binding |
B | 0016310 | biological_process | phosphorylation |
B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
B | 0016791 | molecular_function | phosphatase activity |
B | 0018105 | biological_process | peptidyl-serine phosphorylation |
B | 0050790 | biological_process | regulation of catalytic activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE AMP A 1604 |
Chain | Residue |
A | ASN104 |
A | ASN377 |
A | SER105 |
A | HIS113 |
A | LEU116 |
A | LYS291 |
A | LYS294 |
A | THR295 |
A | TYR298 |
A | GLU376 |
site_id | AC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE ATP A 1605 |
Chain | Residue |
A | PRO316 |
A | GLY317 |
A | ILE318 |
A | VAL322 |
A | MET323 |
A | VAL325 |
A | LYS336 |
A | GLU416 |
A | ARG417 |
A | ARG418 |
A | MET419 |
A | PRO421 |
A | ASN462 |
A | TYR474 |
A | ASP475 |
A | ASP477 |
A | GLU478 |
A | MG1606 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 1606 |
Chain | Residue |
A | ASN462 |
A | ASP475 |
A | ATP1605 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE AMP B 1604 |
Chain | Residue |
B | ASN104 |
B | SER105 |
B | HIS113 |
B | LEU116 |
B | LYS291 |
B | LYS294 |
B | THR295 |
B | TYR298 |
B | GLU376 |
B | ASN377 |
B | HOH580 |
site_id | AC5 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE ATP B 1605 |
Chain | Residue |
B | PRO316 |
B | GLY317 |
B | ILE318 |
B | VAL322 |
B | MET323 |
B | VAL325 |
B | VAL334 |
B | LYS336 |
B | GLU416 |
B | ARG417 |
B | ARG418 |
B | MET419 |
B | PRO421 |
B | ASN462 |
B | TYR474 |
B | ASP475 |
B | ASP477 |
B | GLU478 |
B | HOH594 |
B | MG1606 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 1606 |
Chain | Residue |
B | ASN462 |
B | ASP475 |
B | ATP1605 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00747 |
Chain | Residue | Details |
A | ASP371 | |
B | ASP371 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00747 |
Chain | Residue | Details |
A | ALA315 | |
A | LYS336 | |
B | ALA315 | |
B | LYS336 |