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1BO5

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_idFB1
Number of Residues6
DetailsFBP BINDING SITE
ChainResidue
OGLY234
OTHR235
OARG236
ZGLY234
ZTHR235
ZARG236

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
ZTYR135
ZASP245
ZGLU478
OASP245
OGLU478
ZTHR13
ZARG83
ZGLU84
OARG83
OGLU84
OTYR135
OTHR13

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
OTHR14
OGLY411
ZTHR14
ZGLY411

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:10090737, ECO:0007744|PDB:1GLJ
ChainResidueDetails
OSER15
ZSER15

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
OARG17
ZARG17

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:9843423, ECO:0007744|PDB:1BO5
ChainResidueDetails
OGLY234
OARG236
ZGLY234
ZARG236

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
OGLN246
ZGLN246

site_idSWS_FT_FI7
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:10090737, ECO:0007744|PDB:1BWF, ECO:0007744|PDB:1GLL
ChainResidueDetails
OTHR267
OGLY310
OGLN314
ZTHR267
ZGLY310
ZGLN314

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
OASN415
ZASN415

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-malonyllysine => ECO:0000269|PubMed:21908771
ChainResidueDetails
OLYS232
ZLYS232

219869

PDB entries from 2024-05-15

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