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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8D44

Cryo-electron microscopy structure of human kidney Fructose-bisphosphate aldolase B

Functional Information from GO Data
ChainGOidnamespacecontents
A0004332molecular_functionfructose-bisphosphate aldolase activity
A0005515molecular_functionprotein binding
A0005815cellular_componentmicrotubule organizing center
A0005829cellular_componentcytosol
A0006000biological_processfructose metabolic process
A0006001biological_processfructose catabolic process
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0008092molecular_functioncytoskeletal protein binding
A0016829molecular_functionlyase activity
A0030388biological_processfructose 1,6-bisphosphate metabolic process
A0034451cellular_componentcentriolar satellite
A0042802molecular_functionidentical protein binding
A0051117molecular_functionATPase binding
A0060090molecular_functionmolecular adaptor activity
A0061609molecular_functionfructose-1-phosphate aldolase activity
A0061624biological_processfructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate
A0070061molecular_functionfructose binding
A0070062cellular_componentextracellular exosome
A0070072biological_processvacuolar proton-transporting V-type ATPase complex assembly
A1905856biological_processnegative regulation of pentose-phosphate shunt
B0004332molecular_functionfructose-bisphosphate aldolase activity
B0005515molecular_functionprotein binding
B0005815cellular_componentmicrotubule organizing center
B0005829cellular_componentcytosol
B0006000biological_processfructose metabolic process
B0006001biological_processfructose catabolic process
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0008092molecular_functioncytoskeletal protein binding
B0016829molecular_functionlyase activity
B0030388biological_processfructose 1,6-bisphosphate metabolic process
B0034451cellular_componentcentriolar satellite
B0042802molecular_functionidentical protein binding
B0051117molecular_functionATPase binding
B0060090molecular_functionmolecular adaptor activity
B0061609molecular_functionfructose-1-phosphate aldolase activity
B0061624biological_processfructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate
B0070061molecular_functionfructose binding
B0070062cellular_componentextracellular exosome
B0070072biological_processvacuolar proton-transporting V-type ATPase complex assembly
B1905856biological_processnegative regulation of pentose-phosphate shunt
C0004332molecular_functionfructose-bisphosphate aldolase activity
C0005515molecular_functionprotein binding
C0005815cellular_componentmicrotubule organizing center
C0005829cellular_componentcytosol
C0006000biological_processfructose metabolic process
C0006001biological_processfructose catabolic process
C0006094biological_processgluconeogenesis
C0006096biological_processglycolytic process
C0008092molecular_functioncytoskeletal protein binding
C0016829molecular_functionlyase activity
C0030388biological_processfructose 1,6-bisphosphate metabolic process
C0034451cellular_componentcentriolar satellite
C0042802molecular_functionidentical protein binding
C0051117molecular_functionATPase binding
C0060090molecular_functionmolecular adaptor activity
C0061609molecular_functionfructose-1-phosphate aldolase activity
C0061624biological_processfructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate
C0070061molecular_functionfructose binding
C0070062cellular_componentextracellular exosome
C0070072biological_processvacuolar proton-transporting V-type ATPase complex assembly
C1905856biological_processnegative regulation of pentose-phosphate shunt
D0004332molecular_functionfructose-bisphosphate aldolase activity
D0005515molecular_functionprotein binding
D0005815cellular_componentmicrotubule organizing center
D0005829cellular_componentcytosol
D0006000biological_processfructose metabolic process
D0006001biological_processfructose catabolic process
D0006094biological_processgluconeogenesis
D0006096biological_processglycolytic process
D0008092molecular_functioncytoskeletal protein binding
D0016829molecular_functionlyase activity
D0030388biological_processfructose 1,6-bisphosphate metabolic process
D0034451cellular_componentcentriolar satellite
D0042802molecular_functionidentical protein binding
D0051117molecular_functionATPase binding
D0060090molecular_functionmolecular adaptor activity
D0061609molecular_functionfructose-1-phosphate aldolase activity
D0061624biological_processfructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate
D0070061molecular_functionfructose binding
D0070062cellular_componentextracellular exosome
D0070072biological_processvacuolar proton-transporting V-type ATPase complex assembly
D1905856biological_processnegative regulation of pentose-phosphate shunt
Functional Information from PROSITE/UniProt
site_idPS00158
Number of Residues11
DetailsALDOLASE_CLASS_I Fructose-bisphosphate aldolase class-I active site. VyLEGtLLKPN
ChainResidueDetails
DVAL222-ASN232
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":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"Q91Y97","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues12
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q91Y97","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues24
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues8
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00884","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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