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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2FUA

L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T WITH COBALT

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0005996biological_processmonosaccharide metabolic process
A0006004biological_processfucose metabolic process
A0008270molecular_functionzinc ion binding
A0008738molecular_functionL-fuculose-phosphate aldolase activity
A0016829molecular_functionlyase activity
A0016832molecular_functionaldehyde-lyase activity
A0019317biological_processfucose catabolic process
A0019323biological_processpentose catabolic process
A0019568biological_processarabinose catabolic process
A0019571biological_processD-arabinose catabolic process
A0042355biological_processL-fucose catabolic process
A0046872molecular_functionmetal ion binding
A0046914molecular_functiontransition metal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 216
ChainResidue
AGLU73
AHIS92
AHIS94
ATYR113
AHIS155
site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 300
ChainResidue
AASN29
ATHR43
ASER71
ASER72
AHOH401
AHOH417
AHOH444
AHOH449
site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
AHIS64
AGLU66
AGLY67
ATRP74
AARG75
ATYR209
AHOH476
AHOH478
AHOH503
AHOH506
site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME A 302
ChainResidue
ACYS14
AGLY28
AILE45
AHOH417
site_idACT
Number of Residues5
DetailsTHE ACTIVE SITE IS DEFINED BY THE COBALT ION AND THE FOUR COBALT COORDINATING RESIDUES.
ChainResidue
ACO216
AGLU73
AHIS92
AHIS94
AHIS155
site_idPBS
Number of Residues5
DetailsTHE PHOSPHATE BINDING SITE NEAR THE ACTIVE CENTER IS OCCUPIED BY A SULFATE ION FROM THE SOLVENT (SO4 300); FIVE RESIDUES ARE INVOLVED IN BINDING OF THE SULFATE.
ChainResidue
AGLY44
ASER71
ASER72
AASN29
ATHR43
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"10821675","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11054289","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11054289","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8676381","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E47","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E48","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FUA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00987","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10821675","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11054289","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15299567","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8676381","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DZU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DZV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DZW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DZX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DZY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DZZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E48","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E49","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E4A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E4B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E4C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FUA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FUA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FUA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00987","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10821675","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11054289","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15299567","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8676381","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DZU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DZV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DZW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DZX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DZY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DZZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E46","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E47","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E48","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E49","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E4A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E4B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E4C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FUA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FUA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FUA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues3
DetailsSite: {"description":"Plays a key role in the stabilization of the transition state and positioning the aldehyde component","evidences":[{"source":"PubMed","id":"10821675","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1fua
ChainResidueDetails
ATYR113
AGLU73
site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fua
ChainResidueDetails
AALA117
site_idMCSA1
Number of Residues6
DetailsM-CSA 72
ChainResidueDetails
AGLU73hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS92metal ligand
AHIS94metal ligand
ATYR113electrostatic stabiliser, transition state stabiliser
AHIS155metal ligand
ATYR209electrostatic stabiliser, transition state stabiliser

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PDB entries from 2025-12-10

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