3LKK
Crystal structure of the isopentenyl phosphate kinase substrate complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004349 | molecular_function | glutamate 5-kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005829 | cellular_component | cytosol |
A | 0006561 | biological_process | proline biosynthetic process |
A | 0008299 | biological_process | isoprenoid biosynthetic process |
A | 0016301 | molecular_function | kinase activity |
A | 0102043 | molecular_function | isopentenyl phosphate kinase activity |
B | 0004349 | molecular_function | glutamate 5-kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005829 | cellular_component | cytosol |
B | 0006561 | biological_process | proline biosynthetic process |
B | 0008299 | biological_process | isoprenoid biosynthetic process |
B | 0016301 | molecular_function | kinase activity |
B | 0102043 | molecular_function | isopentenyl phosphate kinase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE ATP A 246 |
Chain | Residue |
A | LYS5 |
A | ASP164 |
A | GLY167 |
A | TYR169 |
A | LYS171 |
A | ASP172 |
A | PRO173 |
A | LYS174 |
A | LYS205 |
A | IP8247 |
A | HOH287 |
A | GLY7 |
A | HOH357 |
A | HOH361 |
A | GLY8 |
A | SER9 |
A | LYS14 |
A | GLY44 |
A | GLY45 |
A | GLY46 |
A | HIS50 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE IP8 A 247 |
Chain | Residue |
A | LYS5 |
A | GLY44 |
A | GLY45 |
A | GLY49 |
A | HIS50 |
A | GLY128 |
A | SER142 |
A | GLY143 |
A | ATP246 |
A | HOH292 |
site_id | AC3 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE ATP B 246 |
Chain | Residue |
B | LYS5 |
B | GLY7 |
B | GLY8 |
B | SER9 |
B | LYS14 |
B | GLY44 |
B | GLY45 |
B | GLY46 |
B | HIS50 |
B | ASP164 |
B | VAL165 |
B | GLY167 |
B | TYR169 |
B | LYS171 |
B | ASP172 |
B | PRO173 |
B | LYS174 |
B | ILE202 |
B | LYS205 |
B | IP8247 |
B | HOH272 |
B | HOH330 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE IP8 B 247 |
Chain | Residue |
B | LYS5 |
B | GLY44 |
B | GLY45 |
B | GLY49 |
B | HIS50 |
B | GLY128 |
B | ASP129 |
B | SER142 |
B | GLY143 |
B | ATP246 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 18 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS5 | |
B | LYS5 | |
B | GLY45 | |
B | GLY46 | |
B | HIS50 | |
B | GLY143 | |
B | ASP164 | |
B | TYR169 | |
B | GLY201 | |
B | LYS205 | |
A | GLY45 | |
A | GLY46 | |
A | HIS50 | |
A | GLY143 | |
A | ASP164 | |
A | TYR169 | |
A | GLY201 | |
A | LYS205 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | LYS14 | |
B | LYS14 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 1004 |
Chain | Residue | Details |
A | LYS5 | electrostatic stabiliser, transition state stabiliser |
A | GLY8 | hydrogen bond donor, transition state stabiliser |
A | LYS14 | electrostatic stabiliser, transition state stabiliser |
A | GLY45 | hydrogen bond donor, transition state stabiliser |
A | HIS50 | electrostatic interaction, electrostatic stabiliser, transition state stabiliser |
A | ASP144 | electrostatic stabiliser, transition state stabiliser |
A | THR163 | hydrogen bond donor, transition state stabiliser |
A | LYS205 | electrostatic stabiliser, transition state stabiliser |