Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3PNK

Crystal Structure of E.coli Dha kinase DhaK

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 Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1228
ChainResidue
AGLY52
AGLY53
AHIS56
APHE78
ASER80
ALYS104
AASP109
AHIS218
AHOH420

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 1228
ChainResidue
BGLY52
BGLY53
BHIS56
BPHE78
BLYS104
BASP109
BHIS218
BHOH419

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:21209328
ChainResidueDetails
AHIS56
BHIS56

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
AHIS218
BHIS218

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
AGLY53
AASP109
BGLY53
BASP109

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
ALYS104
BLYS104

223790

PDB entries from 2024-08-14

PDB statisticsPDBj update infoContact PDBjnumon