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CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN ESCHERICHIA COLI GLYCEROL KINASE AND THE ALLOSTERIC REGULATOR FRUCTOSE 1,6-BISPHOSPHATE.

Functional Information from GO Data
ChainGOidnamespacecontents
O0004370molecular_functionglycerol kinase activity
O0005515molecular_functionprotein binding
O0005524molecular_functionATP binding
O0005829cellular_componentcytosol
O0005975biological_processcarbohydrate metabolic process
O0006071biological_processglycerol metabolic process
O0006072biological_processglycerol-3-phosphate metabolic process
O0006974biological_processDNA damage response
O0008270molecular_functionzinc ion binding
O0016301molecular_functionkinase activity
O0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
O0019563biological_processglycerol catabolic process
O0042802molecular_functionidentical protein binding
O0046872molecular_functionmetal ion binding
Z0004370molecular_functionglycerol kinase activity
Z0005515molecular_functionprotein binding
Z0005524molecular_functionATP binding
Z0005829cellular_componentcytosol
Z0005975biological_processcarbohydrate metabolic process
Z0006071biological_processglycerol metabolic process
Z0006072biological_processglycerol-3-phosphate metabolic process
Z0006974biological_processDNA damage response
Z0008270molecular_functionzinc ion binding
Z0016301molecular_functionkinase activity
Z0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
Z0019563biological_processglycerol catabolic process
Z0042802molecular_functionidentical protein binding
Z0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EPE O 602
ChainResidue
OHIS179
OASP198
OTRP199
OARG211
OGLU212
OLEU214
OPRO215
OGLU216
OVAL217

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL O 601
ChainResidue
OARG83
OGLU84
OTRP103
OTYR135
OASP245
OGLN246
OPHE270

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL Z 603
ChainResidue
ZARG83
ZGLU84
ZTRP103
ZTYR135
ZASP245
ZGLN246
ZPHE270

Functional Information from PROSITE/UniProt
site_idPS00445
Number of Residues21
DetailsFGGY_KINASES_2 FGGY family of carbohydrate kinases signature 2. GaIFGLtrgvnan.HIIRATLE
ChainResidueDetails
OGLY362-GLU382

site_idPS00933
Number of Residues13
DetailsFGGY_KINASES_1 FGGY family of carbohydrate kinases signature 1. YfSgtKVKWILDH
ChainResidueDetails
OTYR135-HIS147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:8170944, ECO:0007744|PDB:1GLC, ECO:0007744|PDB:1GLD, ECO:0007744|PDB:1GLE
ChainResidueDetails
OTHR14
OGLU84
OTHR85
OPHE136
ZPHE136
ZGLN246
ZARG479
OGLN246
OARG479
ZTHR14
ZGLU84
ZTHR85

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:10090737, ECO:0007744|PDB:1BWF, ECO:0007744|PDB:1GLJ, ECO:0007744|PDB:1GLL
ChainResidueDetails
ZSER15
ZALA412
OSER15
OALA412

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:10090737, ECO:0007744|PDB:1GLJ
ChainResidueDetails
OSER16
ZSER16

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: 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
ChainResidueDetails
OALA18
ZALA18

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:9843423, ECO:0007744|PDB:1BO5
ChainResidueDetails
OTHR235
OILE237
ZTHR235
ZILE237

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8430315, ECO:0000269|PubMed:9843423, ECO:0007744|PDB:1BO5, ECO:0007744|PDB:1BOT
ChainResidueDetails
OGLN247
ZGLN247

site_idSWS_FT_FI7
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:10090737, ECO:0007744|PDB:1BWF, ECO:0007744|PDB:1GLL
ChainResidueDetails
OGLY268
OALA311
OTRP315
ZGLY268
ZALA311
ZTRP315

site_idSWS_FT_FI8
Number of Residues2
DetailsBINDING: 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
ChainResidueDetails
OASN416
ZASN416

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-malonyllysine => ECO:0000269|PubMed:21908771
ChainResidueDetails
OGLY233
ZGLY233

219869

PDB entries from 2024-05-15

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