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1UN8

Crystal structure of the dihydroxyacetone kinase of C. freundii (native form)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004371molecular_functionglycerone kinase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006071biological_processglycerol metabolic process
A0008289molecular_functionlipid binding
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0019563biological_processglycerol catabolic process
A0019588biological_processanaerobic glycerol catabolic process
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0004371molecular_functionglycerone kinase activity
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006071biological_processglycerol metabolic process
B0008289molecular_functionlipid binding
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016740molecular_functiontransferase activity
B0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
B0019563biological_processglycerol catabolic process
B0019588biological_processanaerobic glycerol catabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MYY A1551
ChainResidue
AVAL365
ALEU546
ALEU369
AALA395
ALEU413
AILE420
AMET436
APHE440
AVAL453
APRO492

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MYY B1551
ChainResidue
BILE361
BLEU369
BPHE392
BALA395
BMET436
BPHE440
BVAL453
BPRO492
BLEU546
BHOH2109

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Tele-hemiaminal-histidine intermediate => ECO:0000255|PROSITE-ProRule:PRU00814, ECO:0000269|PubMed:12966101
ChainResidueDetails
AHIS220
BHIS220

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AGLY58
ALYS109
AASP114
BGLY58
BLYS109
BASP114

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:12966101
ChainResidueDetails
AASP385
BASP533
ASER431
AGLY468
ATHR476
AASP533
BASP385
BSER431
BGLY468
BTHR476

218853

PDB entries from 2024-04-24

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