6K5L
The crystal structure of isocitrate dehydrogenase kinase/phosphatase wtih two Mn2+ from E. coli
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0004721 | molecular_function | phosphoprotein phosphatase activity |
A | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
A | 0005515 | molecular_function | protein binding |
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 | 0008772 | molecular_function | [isocitrate dehydrogenase (NADP+)] kinase activity |
A | 0016208 | molecular_function | AMP binding |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0016740 | molecular_function | transferase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
A | 0016791 | molecular_function | phosphatase activity |
A | 0030145 | molecular_function | manganese ion binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004674 | molecular_function | protein serine/threonine kinase activity |
B | 0004721 | molecular_function | phosphoprotein phosphatase activity |
B | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
B | 0005515 | molecular_function | protein binding |
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 | 0008772 | molecular_function | [isocitrate dehydrogenase (NADP+)] kinase activity |
B | 0016208 | molecular_function | AMP binding |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
B | 0016740 | molecular_function | transferase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
B | 0016791 | molecular_function | phosphatase activity |
B | 0030145 | molecular_function | manganese ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | binding site for residue AMP A 1001 |
Chain | Residue |
A | ASN104 |
A | GLU376 |
A | ASN377 |
A | HOH1111 |
A | HOH1114 |
A | HOH1124 |
A | HOH1130 |
A | HOH1160 |
A | SER105 |
A | HIS113 |
A | LEU116 |
A | LEU121 |
A | LYS291 |
A | LYS294 |
A | THR295 |
A | TYR298 |
site_id | AC2 |
Number of Residues | 21 |
Details | binding site for residue ADP A 1002 |
Chain | Residue |
A | PRO316 |
A | GLY317 |
A | ILE318 |
A | GLY320 |
A | MET321 |
A | VAL322 |
A | MET323 |
A | VAL325 |
A | LYS336 |
A | GLU416 |
A | ARG417 |
A | ARG418 |
A | MET419 |
A | ASN462 |
A | TYR474 |
A | ASP475 |
A | ASP477 |
A | MN1003 |
A | MN1004 |
A | HOH1120 |
A | HOH1156 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue MN A 1003 |
Chain | Residue |
A | ASN462 |
A | ASP475 |
A | ADP1002 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue MN A 1004 |
Chain | Residue |
A | ASP475 |
A | ASP477 |
A | ADP1002 |
A | HOH1135 |
site_id | AC5 |
Number of Residues | 13 |
Details | binding site for residue AMP B 1001 |
Chain | Residue |
B | ASN104 |
B | SER105 |
B | HIS113 |
B | LEU116 |
B | LEU121 |
B | LYS291 |
B | LYS294 |
B | THR295 |
B | TYR298 |
B | GLU376 |
B | ASN377 |
B | HOH1110 |
B | HOH1134 |
site_id | AC6 |
Number of Residues | 18 |
Details | binding site for residue ADP B 1002 |
Chain | Residue |
B | PRO316 |
B | GLY317 |
B | ILE318 |
B | GLY320 |
B | MET321 |
B | VAL322 |
B | MET323 |
B | VAL325 |
B | LYS336 |
B | GLU416 |
B | ARG417 |
B | MET419 |
B | ASN462 |
B | TYR474 |
B | ASP475 |
B | ASP477 |
B | MN1003 |
B | MN1004 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue MN B 1003 |
Chain | Residue |
B | ASN462 |
B | ASP475 |
B | ADP1002 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue MN B 1004 |
Chain | Residue |
B | LYS346 |
B | ASP475 |
B | ASP477 |
B | ADP1002 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000305 |
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 |