1BOT
CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN ESCHERICHIA COLI GLYCEROL KINASE AND THE ALLOSTERIC REGULATOR FRUCTOSE 1,6-BISPHOSPHATE.
Functional Information from GO Data
Chain | GOid | namespace | contents |
O | 0004370 | molecular_function | glycerol kinase activity |
O | 0005515 | molecular_function | protein binding |
O | 0005524 | molecular_function | ATP binding |
O | 0005829 | cellular_component | cytosol |
O | 0005975 | biological_process | carbohydrate metabolic process |
O | 0006071 | biological_process | glycerol metabolic process |
O | 0006072 | biological_process | glycerol-3-phosphate metabolic process |
O | 0006974 | biological_process | DNA damage response |
O | 0008270 | molecular_function | zinc ion binding |
O | 0016301 | molecular_function | kinase activity |
O | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
O | 0019563 | biological_process | glycerol catabolic process |
O | 0042802 | molecular_function | identical protein binding |
O | 0046872 | molecular_function | metal ion binding |
Z | 0004370 | molecular_function | glycerol kinase activity |
Z | 0005515 | molecular_function | protein binding |
Z | 0005524 | molecular_function | ATP binding |
Z | 0005829 | cellular_component | cytosol |
Z | 0005975 | biological_process | carbohydrate metabolic process |
Z | 0006071 | biological_process | glycerol metabolic process |
Z | 0006072 | biological_process | glycerol-3-phosphate metabolic process |
Z | 0006974 | biological_process | DNA damage response |
Z | 0008270 | molecular_function | zinc ion binding |
Z | 0016301 | molecular_function | kinase activity |
Z | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
Z | 0019563 | biological_process | glycerol catabolic process |
Z | 0042802 | molecular_function | identical protein binding |
Z | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EPE O 602 |
Chain | Residue |
O | HIS179 |
O | ASP198 |
O | TRP199 |
O | ARG211 |
O | GLU212 |
O | LEU214 |
O | PRO215 |
O | GLU216 |
O | VAL217 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL O 601 |
Chain | Residue |
O | ARG83 |
O | GLU84 |
O | TRP103 |
O | TYR135 |
O | ASP245 |
O | GLN246 |
O | PHE270 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL Z 603 |
Chain | Residue |
Z | ARG83 |
Z | GLU84 |
Z | TRP103 |
Z | TYR135 |
Z | ASP245 |
Z | GLN246 |
Z | PHE270 |
Functional Information from PROSITE/UniProt
site_id | PS00445 |
Number of Residues | 21 |
Details | FGGY_KINASES_2 FGGY family of carbohydrate kinases signature 2. GaIFGLtrgvnan.HIIRATLE |
Chain | Residue | Details |
O | GLY362-GLU382 |
site_id | PS00933 |
Number of Residues | 13 |
Details | FGGY_KINASES_1 FGGY family of carbohydrate kinases signature 1. YfSgtKVKWILDH |
Chain | Residue | Details |
O | TYR135-HIS147 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8170944, ECO:0007744|PDB:1GLC, ECO:0007744|PDB:1GLD, ECO:0007744|PDB:1GLE |
Chain | Residue | Details |
O | THR14 | |
Z | PHE136 | |
Z | GLN246 | |
Z | ARG479 | |
O | GLU84 | |
O | THR85 | |
O | PHE136 | |
O | GLN246 | |
O | ARG479 | |
Z | THR14 | |
Z | GLU84 | |
Z | THR85 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:10090737, ECO:0007744|PDB:1BWF, ECO:0007744|PDB:1GLJ, ECO:0007744|PDB:1GLL |
Chain | Residue | Details |
O | SER15 | |
O | ALA412 | |
Z | SER15 | |
Z | ALA412 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:10090737, ECO:0007744|PDB:1GLJ |
Chain | Residue | Details |
O | SER16 | |
Z | SER16 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8170944, ECO:0000269|PubMed:8430315, ECO:0000269|PubMed:9817843, ECO:0007744|PDB:1GLB, ECO:0007744|PDB:1GLD, ECO:0007744|PDB:1GLE, ECO:0007744|PDB:1GLF |
Chain | Residue | Details |
O | ALA18 | |
Z | ALA18 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9843423, ECO:0007744|PDB:1BO5 |
Chain | Residue | Details |
O | THR235 | |
O | ILE237 | |
Z | THR235 | |
Z | ILE237 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8430315, ECO:0000269|PubMed:9843423, ECO:0007744|PDB:1BO5, ECO:0007744|PDB:1BOT |
Chain | Residue | Details |
O | GLN247 | |
Z | GLN247 |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305|PubMed:10090737, ECO:0007744|PDB:1BWF, ECO:0007744|PDB:1GLL |
Chain | Residue | Details |
O | GLY268 | |
O | ALA311 | |
O | TRP315 | |
Z | GLY268 | |
Z | ALA311 | |
Z | TRP315 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8170944, ECO:0000269|PubMed:8430315, ECO:0007744|PDB:1GLB, ECO:0007744|PDB:1GLC, ECO:0007744|PDB:1GLD, ECO:0007744|PDB:1GLE |
Chain | Residue | Details |
O | ASN416 | |
Z | ASN416 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: N6-malonyllysine => ECO:0000269|PubMed:21908771 |
Chain | Residue | Details |
O | GLY233 | |
Z | GLY233 |