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3PNL

Crystal Structure of E.coli Dha kinase DhaK-DhaL complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004371molecular_functionglycerone kinase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006071biological_processglycerol metabolic process
A0006090biological_processpyruvate metabolic process
A0006974biological_processDNA damage response
A0016301molecular_functionkinase activity
A0019563biological_processglycerol catabolic process
A0042182biological_processketone catabolic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046365biological_processmonosaccharide catabolic process
A0046835biological_processcarbohydrate phosphorylation
A0047324molecular_functionphosphoenolpyruvate-glycerone phosphotransferase activity
A0061610biological_processglycerol to glycerone phosphate metabolic process
A1990234cellular_componenttransferase complex
B0000287molecular_functionmagnesium ion binding
B0004371molecular_functionglycerone kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006071biological_processglycerol metabolic process
B0006090biological_processpyruvate metabolic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0019563biological_processglycerol catabolic process
B0043531molecular_functionADP binding
B0046835biological_processcarbohydrate phosphorylation
B0046872molecular_functionmetal ion binding
B0047324molecular_functionphosphoenolpyruvate-glycerone phosphotransferase activity
B1990234cellular_componenttransferase complex
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 1228
ChainResidue
AGLY52
BHOH231
AGLY53
AHIS56
APHE78
ASER80
ALYS104
AASP109
AHIS218
BARG178

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE ADP B 1211
ChainResidue
ATHR107
AHOH359
BASP30
BASP35
BASP37
BHIS38
BASN41
BGLY78
BALA79
BSER80
BLEU83
BGLY121
BTHR129
BMET130
BGLY177
BASP191
BPRO192
BGLY193
BHOH215
BHOH216
BHOH231
BHOH243
BHOH254
BMG1212
BMG1213

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 1212
ChainResidue
BASP30
BASP35
BASP37
BHOH254
BADP1211
BMG1213

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 1213
ChainResidue
APHE78
BASP35
BASP37
BHOH231
BADP1211
BMG1212

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16647083, ECO:0000269|PubMed:24440518, ECO:0007744|PDB:2BTD, ECO:0007744|PDB:4LRZ
ChainResidueDetails
BASP30

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:16647083, ECO:0000269|PubMed:21209328, ECO:0000269|PubMed:24440518, ECO:0007744|PDB:2BTD, ECO:0007744|PDB:3PNL, ECO:0007744|PDB:4LRZ
ChainResidueDetails
BASP37
BHIS38
BALA79
BGLY121
BMET130
BASP191
BASP35

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16647083, ECO:0000305|PubMed:21209328, ECO:0007744|PDB:2BTD
ChainResidueDetails
BARG178
AASP109

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12813127, ECO:0000269|PubMed:21209328, ECO:0007744|PDB:1OI2, ECO:0007744|PDB:3PNK, ECO:0007744|PDB:3PNL, ECO:0007744|PDB:3PNQ
ChainResidueDetails
ALYS104

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PDB entries from 2024-05-15

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