1BU6
CRYSTAL STRUCTURES OF ESCHERICHIA COLI GLYCEROL KINASE AND THE MUTANT A65T IN AN INACTIVE TETRAMER: CONFORMATIONAL CHANGES AND IMPLICATIONS FOR ALLOSTERIC REGULATION
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 |
X | 0004370 | molecular_function | glycerol kinase activity |
X | 0005515 | molecular_function | protein binding |
X | 0005524 | molecular_function | ATP binding |
X | 0005829 | cellular_component | cytosol |
X | 0005975 | biological_process | carbohydrate metabolic process |
X | 0006071 | biological_process | glycerol metabolic process |
X | 0006072 | biological_process | glycerol-3-phosphate metabolic process |
X | 0006974 | biological_process | DNA damage response |
X | 0008270 | molecular_function | zinc ion binding |
X | 0016301 | molecular_function | kinase activity |
X | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
X | 0019563 | biological_process | glycerol catabolic process |
X | 0042802 | molecular_function | identical protein binding |
X | 0046872 | molecular_function | metal ion binding |
Y | 0004370 | molecular_function | glycerol kinase activity |
Y | 0005515 | molecular_function | protein binding |
Y | 0005524 | molecular_function | ATP binding |
Y | 0005829 | cellular_component | cytosol |
Y | 0005975 | biological_process | carbohydrate metabolic process |
Y | 0006071 | biological_process | glycerol metabolic process |
Y | 0006072 | biological_process | glycerol-3-phosphate metabolic process |
Y | 0006974 | biological_process | DNA damage response |
Y | 0008270 | molecular_function | zinc ion binding |
Y | 0016301 | molecular_function | kinase activity |
Y | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
Y | 0019563 | biological_process | glycerol catabolic process |
Y | 0042802 | molecular_function | identical protein binding |
Y | 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 | 10 |
Details | BINDING SITE FOR RESIDUE SO4 O 502 |
Chain | Residue |
X | HOH506 |
Z | ARG236 |
O | ASN228 |
O | GLY233 |
O | GLY234 |
O | ARG236 |
O | HOH505 |
X | GLY233 |
X | GLY234 |
X | ARG236 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 Z 502 |
Chain | Residue |
O | ARG236 |
Y | GLY233 |
Y | GLY234 |
Y | ARG236 |
Z | GLY233 |
Z | GLY234 |
Z | ARG236 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 O 503 |
Chain | Residue |
O | GLY12 |
O | THR13 |
O | THR14 |
O | ARG17 |
O | THR267 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 Y 502 |
Chain | Residue |
Y | GLY12 |
Y | THR13 |
Y | THR14 |
Y | ASP245 |
Y | THR267 |
Y | GOL503 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 Z 503 |
Chain | Residue |
Z | GLY12 |
Z | THR13 |
Z | ARG17 |
Z | ASP245 |
Z | THR267 |
Z | HOH513 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 X 502 |
Chain | Residue |
X | GLY12 |
X | THR13 |
X | ARG17 |
X | ASP245 |
X | THR267 |
X | GOL503 |
X | HOH513 |
X | HOH526 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL O 504 |
Chain | Residue |
O | ARG83 |
O | GLU84 |
O | TRP103 |
O | TYR135 |
O | ASP245 |
O | GLN246 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL Y 503 |
Chain | Residue |
Y | GLN82 |
Y | ARG83 |
Y | GLU84 |
Y | TRP103 |
Y | TYR135 |
Y | ASP245 |
Y | GLN246 |
Y | SO4502 |
Y | HOH527 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL Z 504 |
Chain | Residue |
Z | GLN82 |
Z | ARG83 |
Z | GLU84 |
Z | TRP103 |
Z | TYR135 |
Z | ASP245 |
Z | GLN246 |
Z | PHE270 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL X 503 |
Chain | Residue |
X | GLN82 |
X | ARG83 |
X | GLU84 |
X | TRP103 |
X | TYR135 |
X | ASP245 |
X | GLN246 |
X | SO4502 |
site_id | SO4 |
Number of Residues | 1 |
Details | SULPHATE BINDING SITE. RESIDUES 230 - 236: THIS REGION IS DISORDERED IN PREVIOUSLY SOLVED CRYSTAL STRUCTURES OF GLYCEROL KINASE, BUT IS ORDERED IN THIS STRUCTURE AND FORMS A SULPHATE BINDING SITE AT THE 2-FOLD DIMER-DIMER INTERFACE. THIS SITE IS PROPOSED TO BE PART OF THE BINDING SITE FOR THE ALLOSTERIC EFFECTOR FBP (SEE REF. FOR THIS STRUCTURE). |
Chain | Residue |
O | ARG236 |
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 | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8170944, ECO:0007744|PDB:1GLC, ECO:0007744|PDB:1GLD, ECO:0007744|PDB:1GLE |
Chain | Residue | Details |
O | THR14 | |
Y | PHE136 | |
Y | GLN246 | |
Y | ARG479 | |
Z | THR14 | |
Z | GLU84 | |
Z | THR85 | |
Z | PHE136 | |
Z | GLN246 | |
Z | ARG479 | |
X | THR14 | |
O | GLU84 | |
X | GLU84 | |
X | THR85 | |
X | PHE136 | |
X | GLN246 | |
X | ARG479 | |
O | THR85 | |
O | PHE136 | |
O | GLN246 | |
O | ARG479 | |
Y | THR14 | |
Y | GLU84 | |
Y | THR85 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
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 | |
Y | SER15 | |
Y | ALA412 | |
Z | SER15 | |
Z | ALA412 | |
X | SER15 | |
X | ALA412 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:10090737, ECO:0007744|PDB:1GLJ |
Chain | Residue | Details |
O | SER16 | |
Y | SER16 | |
Z | SER16 | |
X | SER16 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
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 | |
Y | ALA18 | |
Z | ALA18 | |
X | ALA18 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9843423, ECO:0007744|PDB:1BO5 |
Chain | Residue | Details |
O | THR235 | |
O | ILE237 | |
Y | THR235 | |
Y | ILE237 | |
Z | THR235 | |
Z | ILE237 | |
X | THR235 | |
X | ILE237 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8430315, ECO:0000269|PubMed:9843423, ECO:0007744|PDB:1BO5, ECO:0007744|PDB:1BOT |
Chain | Residue | Details |
O | GLN247 | |
Y | GLN247 | |
Z | GLN247 | |
X | GLN247 |
site_id | SWS_FT_FI7 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000305|PubMed:10090737, ECO:0007744|PDB:1BWF, ECO:0007744|PDB:1GLL |
Chain | Residue | Details |
O | GLY268 | |
X | GLY268 | |
X | ALA311 | |
X | TRP315 | |
O | ALA311 | |
O | TRP315 | |
Y | GLY268 | |
Y | ALA311 | |
Y | TRP315 | |
Z | GLY268 | |
Z | ALA311 | |
Z | TRP315 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
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 | |
Y | ASN416 | |
Z | ASN416 | |
X | ASN416 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: N6-malonyllysine => ECO:0000269|PubMed:21908771 |
Chain | Residue | Details |
O | GLY233 | |
Y | GLY233 | |
Z | GLY233 | |
X | GLY233 |