2J5V
GLUTAMATE 5-KINASE FROM ESCHERICHIA COLI COMPLEXED WITH GLUTAMYL-5-PHOSPHATE AND PYROGLUTAMIC ACID
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003723 | molecular_function | RNA binding |
A | 0004349 | molecular_function | glutamate 5-kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006561 | biological_process | proline biosynthetic process |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0055129 | biological_process | L-proline biosynthetic process |
A | 1901973 | molecular_function | proline binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003723 | molecular_function | RNA binding |
B | 0004349 | molecular_function | glutamate 5-kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006561 | biological_process | proline biosynthetic process |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0055129 | biological_process | L-proline biosynthetic process |
B | 1901973 | molecular_function | proline binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A1368 |
Chain | Residue |
A | LYS10 |
A | GLY12 |
A | LEU168 |
A | SO41371 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A1371 |
Chain | Residue |
A | LYS217 |
A | MG1368 |
A | RGP1370 |
A | HOH2088 |
A | HOH2089 |
A | LYS10 |
A | GLY12 |
A | THR13 |
A | SER14 |
A | VAL15 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 B1370 |
Chain | Residue |
B | LYS10 |
B | GLY12 |
B | THR13 |
B | SER14 |
B | VAL15 |
B | ASP170 |
B | LYS217 |
B | RGP1369 |
B | HOH2075 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PCA A1369 |
Chain | Residue |
A | THR13 |
A | SER50 |
A | GLY51 |
A | ALA52 |
A | ILE53 |
A | ASN134 |
A | RGP1370 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE RGP A1370 |
Chain | Residue |
A | LYS10 |
A | GLY12 |
A | THR13 |
A | SER50 |
A | GLU135 |
A | ASP137 |
A | LYS145 |
A | ASP148 |
A | ASN149 |
A | PCA1369 |
A | SO41371 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PCA B1368 |
Chain | Residue |
B | THR13 |
B | SER50 |
B | GLY51 |
B | ALA52 |
B | ILE53 |
B | ALA54 |
B | ASN134 |
B | ASP137 |
B | RGP1369 |
site_id | AC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE RGP B1369 |
Chain | Residue |
B | LYS10 |
B | GLY12 |
B | THR13 |
B | SER50 |
B | GLU135 |
B | ASP137 |
B | GLY147 |
B | ASP148 |
B | ASN149 |
B | ASP150 |
B | PCA1368 |
B | SO41370 |
Functional Information from PROSITE/UniProt
site_id | PS00902 |
Number of Residues | 18 |
Details | GLUTAMATE_5_KINASE Glutamate 5-kinase signature. SglGtGGMsTKLqAAdvA |
Chain | Residue | Details |
A | SER207-ALA224 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | LYS10 | |
A | THR169 | |
A | THR211 | |
B | LYS10 | |
B | THR169 | |
B | THR211 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17321544, ECO:0007744|PDB:2J5T, ECO:0007744|PDB:2J5V |
Chain | Residue | Details |
A | SER50 | |
A | ASP137 | |
A | ASN149 | |
B | SER50 | |
B | ASP137 | |
B | ASN149 |