Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5KY6

Human muscle fructose-1,6-bisphosphate aldolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0003779molecular_functionactin binding
A0004332molecular_functionfructose-bisphosphate aldolase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0006000biological_processfructose metabolic process
A0006096biological_processglycolytic process
A0006754biological_processATP biosynthetic process
A0006941biological_processstriated muscle contraction
A0007015biological_processactin filament organization
A0007339biological_processbinding of sperm to zona pellucida
A0008092molecular_functioncytoskeletal protein binding
A0008360biological_processregulation of cell shape
A0015629cellular_componentactin cytoskeleton
A0015631molecular_functiontubulin binding
A0016020cellular_componentmembrane
A0016829molecular_functionlyase activity
A0030388biological_processfructose 1,6-bisphosphate metabolic process
A0031093cellular_componentplatelet alpha granule lumen
A0031430cellular_componentM band
A0031674cellular_componentI band
A0034774cellular_componentsecretory granule lumen
A0035774biological_processpositive regulation of insulin secretion involved in cellular response to glucose stimulus
A0042802molecular_functionidentical protein binding
A0045296molecular_functioncadherin binding
A0046716biological_processmuscle cell cellular homeostasis
A0051289biological_processprotein homotetramerization
A0061621biological_processcanonical glycolysis
A0061827cellular_componentsperm head
A0070061molecular_functionfructose binding
A0070062cellular_componentextracellular exosome
A1904724cellular_componenttertiary granule lumen
A1904813cellular_componentficolin-1-rich granule lumen
B0003723molecular_functionRNA binding
B0003779molecular_functionactin binding
B0004332molecular_functionfructose-bisphosphate aldolase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005829cellular_componentcytosol
B0006000biological_processfructose metabolic process
B0006096biological_processglycolytic process
B0006754biological_processATP biosynthetic process
B0006941biological_processstriated muscle contraction
B0007015biological_processactin filament organization
B0007339biological_processbinding of sperm to zona pellucida
B0008092molecular_functioncytoskeletal protein binding
B0008360biological_processregulation of cell shape
B0015629cellular_componentactin cytoskeleton
B0015631molecular_functiontubulin binding
B0016020cellular_componentmembrane
B0016829molecular_functionlyase activity
B0030388biological_processfructose 1,6-bisphosphate metabolic process
B0031093cellular_componentplatelet alpha granule lumen
B0031430cellular_componentM band
B0031674cellular_componentI band
B0034774cellular_componentsecretory granule lumen
B0035774biological_processpositive regulation of insulin secretion involved in cellular response to glucose stimulus
B0042802molecular_functionidentical protein binding
B0045296molecular_functioncadherin binding
B0046716biological_processmuscle cell cellular homeostasis
B0051289biological_processprotein homotetramerization
B0061621biological_processcanonical glycolysis
B0061827cellular_componentsperm head
B0070061molecular_functionfructose binding
B0070062cellular_componentextracellular exosome
B1904724cellular_componenttertiary granule lumen
B1904813cellular_componentficolin-1-rich granule lumen
C0003723molecular_functionRNA binding
C0003779molecular_functionactin binding
C0004332molecular_functionfructose-bisphosphate aldolase activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005634cellular_componentnucleus
C0005829cellular_componentcytosol
C0006000biological_processfructose metabolic process
C0006096biological_processglycolytic process
C0006754biological_processATP biosynthetic process
C0006941biological_processstriated muscle contraction
C0007015biological_processactin filament organization
C0007339biological_processbinding of sperm to zona pellucida
C0008092molecular_functioncytoskeletal protein binding
C0008360biological_processregulation of cell shape
C0015629cellular_componentactin cytoskeleton
C0015631molecular_functiontubulin binding
C0016020cellular_componentmembrane
C0016829molecular_functionlyase activity
C0030388biological_processfructose 1,6-bisphosphate metabolic process
C0031093cellular_componentplatelet alpha granule lumen
C0031430cellular_componentM band
C0031674cellular_componentI band
C0034774cellular_componentsecretory granule lumen
C0035774biological_processpositive regulation of insulin secretion involved in cellular response to glucose stimulus
C0042802molecular_functionidentical protein binding
C0045296molecular_functioncadherin binding
C0046716biological_processmuscle cell cellular homeostasis
C0051289biological_processprotein homotetramerization
C0061621biological_processcanonical glycolysis
C0061827cellular_componentsperm head
C0070061molecular_functionfructose binding
C0070062cellular_componentextracellular exosome
C1904724cellular_componenttertiary granule lumen
C1904813cellular_componentficolin-1-rich granule lumen
D0003723molecular_functionRNA binding
D0003779molecular_functionactin binding
D0004332molecular_functionfructose-bisphosphate aldolase activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005634cellular_componentnucleus
D0005829cellular_componentcytosol
D0006000biological_processfructose metabolic process
D0006096biological_processglycolytic process
D0006754biological_processATP biosynthetic process
D0006941biological_processstriated muscle contraction
D0007015biological_processactin filament organization
D0007339biological_processbinding of sperm to zona pellucida
D0008092molecular_functioncytoskeletal protein binding
D0008360biological_processregulation of cell shape
D0015629cellular_componentactin cytoskeleton
D0015631molecular_functiontubulin binding
D0016020cellular_componentmembrane
D0016829molecular_functionlyase activity
D0030388biological_processfructose 1,6-bisphosphate metabolic process
D0031093cellular_componentplatelet alpha granule lumen
D0031430cellular_componentM band
D0031674cellular_componentI band
D0034774cellular_componentsecretory granule lumen
D0035774biological_processpositive regulation of insulin secretion involved in cellular response to glucose stimulus
D0042802molecular_functionidentical protein binding
D0045296molecular_functioncadherin binding
D0046716biological_processmuscle cell cellular homeostasis
D0051289biological_processprotein homotetramerization
D0061621biological_processcanonical glycolysis
D0061827cellular_componentsperm head
D0070061molecular_functionfructose binding
D0070062cellular_componentextracellular exosome
D1904724cellular_componenttertiary granule lumen
D1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PROSITE/UniProt
site_idPS00158
Number of Residues11
DetailsALDOLASE_CLASS_I Fructose-bisphosphate aldolase class-I active site. IyLEGtLLKPN
ChainResidueDetails
AILE221-ASN231
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P00883","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Schiff-base intermediate with dihydroxyacetone-P","evidences":[{"source":"UniProtKB","id":"P00883","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00883","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P05065","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29775581","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"N6-malonyllysine; alternate","evidences":[{"source":"PubMed","id":"21908771","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P05065","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29192674","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsSite: {"description":"Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate"}
ChainResidueDetails

246905

PDB entries from 2025-12-31

PDB statisticsPDBj update infoContact PDBjnumon