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1UOE

Crystal structure of the dihydroxyacetone kinase from E. coli in complex with glyceraldehyde

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
A0016310biological_processphosphorylation
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
B0004371molecular_functionglycerone kinase activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0006071biological_processglycerol metabolic process
B0006090biological_processpyruvate metabolic process
B0006974biological_processDNA damage response
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0019563biological_processglycerol catabolic process
B0042182biological_processketone catabolic process
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046365biological_processmonosaccharide catabolic process
B0046835biological_processcarbohydrate phosphorylation
B0047324molecular_functionphosphoenolpyruvate-glycerone phosphotransferase activity
B0061610biological_processglycerol to glycerone phosphate metabolic process
B1990234cellular_componenttransferase complex
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1370
ChainResidue
AHIS33
APRO34
ASER35
AHOH2230
AHOH2231

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B1370
ChainResidue
BHOH2247
BHIS33
BPRO34
BSER35
BHOH2246

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A1369
ChainResidue
AGLY62
AGLY63
AHIS66
APHE88
ASER90
ATYR116
AASP119
AHIS230

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B1369
ChainResidue
BGLY62
BGLY63
BHIS66
BPHE88
BTHR89
BSER90
BTYR116
BASP119
BHIS230

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:21209328
ChainResidueDetails
AHIS66
BHIS66

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Tele-hemiaminal-histidine intermediate => ECO:0000255|PROSITE-ProRule:PRU00814, ECO:0000269|PubMed:12813127, ECO:0000269|PubMed:15476397, ECO:0000269|PubMed:21209328, ECO:0007744|PDB:1OI2, ECO:0007744|PDB:1UOD, ECO:0007744|PDB:1UOE, ECO:0007744|PDB:3PNK, ECO:0007744|PDB:3PNL, ECO:0007744|PDB:3PNQ
ChainResidueDetails
AASP220
BASP220

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12813127, ECO:0000269|PubMed:15476397, ECO:0000269|PubMed:21209328, ECO:0007744|PDB:1OI2, ECO:0007744|PDB:1UOD, ECO:0007744|PDB:1UOE, ECO:0007744|PDB:3PNK, ECO:0007744|PDB:3PNL, ECO:0007744|PDB:3PNQ
ChainResidueDetails
AGLY63
AASP119
BGLY63
BASP119

site_idSWS_FT_FI4
Number of Residues2
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
ALYS114
BLYS114

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PDB entries from 2024-10-30

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