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1GLL

ESCHERICHIA COLI GLYCEROL KINASE MUTANT WITH BOUND ATP ANALOG SHOWING SUBSTANTIAL DOMAIN MOTION

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
Y0004370molecular_functionglycerol kinase activity
Y0005515molecular_functionprotein binding
Y0005524molecular_functionATP binding
Y0005829cellular_componentcytosol
Y0005975biological_processcarbohydrate metabolic process
Y0006071biological_processglycerol metabolic process
Y0006072biological_processglycerol-3-phosphate metabolic process
Y0006974biological_processDNA damage response
Y0008270molecular_functionzinc ion binding
Y0016301molecular_functionkinase activity
Y0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
Y0019563biological_processglycerol catabolic process
Y0042802molecular_functionidentical protein binding
Y0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsPUTATIVE PROTON ACCEPTOR FROM NUCLEOPHILIC O3 POSITION OF GLYCEROL, CHAIN Y.
ChainResidue
OASP245

site_idAC2
Number of Residues1
DetailsPUTATIVE PROTON ACCEPTOR FROM NUCLEOPHILIC O3 POSITION OF GLYCEROL, CHAIN O.
ChainResidue
YASP245

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG Y 602
ChainResidue
YACP601

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG O 602
ChainResidue
OASP245
OACP601

site_idAC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ACP Y 601
ChainResidue
YTHR267
YGLY310
YALA311
YILE313
YGLN314
YALA326
YTYR327
YSER329
YGLY411
YALA412
YASN415
YMG602
YGLY12
YTHR13
YTHR14
YGLY266

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ACP O 601
ChainResidue
OGLY12
OTHR13
OTHR14
OGLY266
OTHR267
OGLY310
OALA311
OILE313
OGLN314
OGLY411
OASN415
OMG602

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL Y 600
ChainResidue
YGLN82
YARG83
YGLU84
YTYR135
YASP245
YGLN246
YPHE270

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL O 600
ChainResidue
OTHR13
OASN81
OGLN82
OARG83
OGLU84
OTYR135
OASP245
OGLN246

Functional Information from PROSITE/UniProt
site_idPS00445
Number of Residues21
DetailsFGGY_KINASES_2 FGGY family of carbohydrate kinases signature 2. GaIFGLtrgvnan.HIIRATLE
ChainResidueDetails
YGLY362-GLU382

site_idPS00933
Number of Residues13
DetailsFGGY_KINASES_1 FGGY family of carbohydrate kinases signature 1. YfSgtKVKWILDH
ChainResidueDetails
YTYR135-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
YTHR14
YGLU84
OPHE136
OGLN246
OARG479
YGLN246
YARG479
OTHR14
OGLU84
OTHR85
YTHR85
YPHE136

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
OSER15
OALA412
YSER15
YALA412

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:10090737, ECO:0007744|PDB:1GLJ
ChainResidueDetails
YSER16
OSER16

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
YALA18
OALA18

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:9843423, ECO:0007744|PDB:1BO5
ChainResidueDetails
YTHR235
YILE237
OTHR235
OILE237

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
YGLN247
OGLN247

site_idSWS_FT_FI7
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:10090737, ECO:0007744|PDB:1BWF, ECO:0007744|PDB:1GLL
ChainResidueDetails
YGLY268
YALA311
YTRP315
OGLY268
OALA311
OTRP315

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
YASN416
OASN416

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-malonyllysine => ECO:0000269|PubMed:21908771
ChainResidueDetails
YGLY233
OGLY233

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PDB entries from 2024-06-12

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