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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1E4C

L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant S71Q

Functional Information from GO Data
ChainGOidnamespacecontents
P0005829cellular_componentcytosol
P0005996biological_processmonosaccharide metabolic process
P0006004biological_processfucose metabolic process
P0008270molecular_functionzinc ion binding
P0008738molecular_functionL-fuculose-phosphate aldolase activity
P0016829molecular_functionlyase activity
P0016830molecular_functioncarbon-carbon lyase activity
P0016832molecular_functionaldehyde-lyase activity
P0019317biological_processfucose catabolic process
P0019323biological_processpentose catabolic process
P0019568biological_processarabinose catabolic process
P0019571biological_processD-arabinose catabolic process
P0042355biological_processL-fucose catabolic process
P0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 S 301
ChainResidue
PTRP74
PARG75
PHOH411
PHOH479
PHOH456
PHOH436
site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN S 999
ChainResidue
PTYR113
PHIS155
PHOH404
PGLU73
PHIS92
PHIS94
site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME S 314
ChainResidue
PCYS14
PGLY28
PILE45
PTYR47
PHOH425
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289
ChainResidueDetails
PGLU73
site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:4FUA
ChainResidueDetails
PGLY28
PTHR43
PGLN71
site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV, ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX, ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ, ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49, ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B, ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA, ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA, ECO:0007744|PDB:4FUA
ChainResidueDetails
PGLU73
site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV, ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX, ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ, ECO:0007744|PDB:1E46, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49, ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B, ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA, ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA, ECO:0007744|PDB:4FUA
ChainResidueDetails
PHIS92
PHIS94
PHIS155
site_idSWS_FT_FI5
Number of Residues3
DetailsSITE: Plays a key role in the stabilization of the transition state and positioning the aldehyde component => ECO:0000269|PubMed:10821675
ChainResidueDetails
PTYR113
PPHE131
PPHE209
Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1fua
ChainResidueDetails
PTYR113
PGLU73
site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fua
ChainResidueDetails
PALA117
site_idMCSA1
Number of Residues6
DetailsM-CSA 72
ChainResidueDetails
PGLU73hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
PHIS92metal ligand
PHIS94metal ligand
PTYR113electrostatic stabiliser, transition state stabiliser
PHIS155metal ligand
PPHE209electrostatic stabiliser, transition state stabiliser

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PDB entries from 2024-12-18

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