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

1L6W

Fructose-6-phosphate aldolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0006000biological_processfructose metabolic process
A0016832molecular_functionaldehyde-lyase activity
A0042182biological_processketone catabolic process
A0042802molecular_functionidentical protein binding
A0097023molecular_functionfructose 6-phosphate aldolase activity
B0005737cellular_componentcytoplasm
B0005975biological_processcarbohydrate metabolic process
B0006000biological_processfructose metabolic process
B0016832molecular_functionaldehyde-lyase activity
B0042182biological_processketone catabolic process
B0042802molecular_functionidentical protein binding
B0097023molecular_functionfructose 6-phosphate aldolase activity
C0005737cellular_componentcytoplasm
C0005975biological_processcarbohydrate metabolic process
C0006000biological_processfructose metabolic process
C0016832molecular_functionaldehyde-lyase activity
C0042182biological_processketone catabolic process
C0042802molecular_functionidentical protein binding
C0097023molecular_functionfructose 6-phosphate aldolase activity
D0005737cellular_componentcytoplasm
D0005975biological_processcarbohydrate metabolic process
D0006000biological_processfructose metabolic process
D0016832molecular_functionaldehyde-lyase activity
D0042182biological_processketone catabolic process
D0042802molecular_functionidentical protein binding
D0097023molecular_functionfructose 6-phosphate aldolase activity
E0005737cellular_componentcytoplasm
E0005975biological_processcarbohydrate metabolic process
E0006000biological_processfructose metabolic process
E0016832molecular_functionaldehyde-lyase activity
E0042182biological_processketone catabolic process
E0042802molecular_functionidentical protein binding
E0097023molecular_functionfructose 6-phosphate aldolase activity
F0005737cellular_componentcytoplasm
F0005975biological_processcarbohydrate metabolic process
F0006000biological_processfructose metabolic process
F0016832molecular_functionaldehyde-lyase activity
F0042182biological_processketone catabolic process
F0042802molecular_functionidentical protein binding
F0097023molecular_functionfructose 6-phosphate aldolase activity
G0005737cellular_componentcytoplasm
G0005975biological_processcarbohydrate metabolic process
G0006000biological_processfructose metabolic process
G0016832molecular_functionaldehyde-lyase activity
G0042182biological_processketone catabolic process
G0042802molecular_functionidentical protein binding
G0097023molecular_functionfructose 6-phosphate aldolase activity
H0005737cellular_componentcytoplasm
H0005975biological_processcarbohydrate metabolic process
H0006000biological_processfructose metabolic process
H0016832molecular_functionaldehyde-lyase activity
H0042182biological_processketone catabolic process
H0042802molecular_functionidentical protein binding
H0097023molecular_functionfructose 6-phosphate aldolase activity
I0005737cellular_componentcytoplasm
I0005975biological_processcarbohydrate metabolic process
I0006000biological_processfructose metabolic process
I0016832molecular_functionaldehyde-lyase activity
I0042182biological_processketone catabolic process
I0042802molecular_functionidentical protein binding
I0097023molecular_functionfructose 6-phosphate aldolase activity
J0005737cellular_componentcytoplasm
J0005975biological_processcarbohydrate metabolic process
J0006000biological_processfructose metabolic process
J0016832molecular_functionaldehyde-lyase activity
J0042182biological_processketone catabolic process
J0042802molecular_functionidentical protein binding
J0097023molecular_functionfructose 6-phosphate aldolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 250
ChainResidue
AASP6
ATHR27
AASN28
ALYS85
ATYR131
AHOH894
AHOH1760
site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 250
ChainResidue
BASN28
BLYS85
BTYR131
BHOH579
BHOH1762
BASP6
BTHR27
site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL C 250
ChainResidue
CASP6
CTHR26
CTHR27
CASN28
CLYS85
CALA129
CTYR131
CHOH636
CHOH1764
site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL D 250
ChainResidue
DASP6
DTHR27
DASN28
DLYS85
DTYR131
DLEU163
DHOH513
DHOH1767
site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL E 250
ChainResidue
EASP6
ETHR27
EASN28
ELYS85
ETYR131
EHOH1768
site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL F 250
ChainResidue
FASP6
FTHR27
FASN28
FLYS85
FTYR131
FHOH663
FHOH1771
site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL G 250
ChainResidue
GASP6
GTHR27
GASN28
GLYS85
GTYR131
GHOH614
GHOH1772
site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL H 250
ChainResidue
HASP6
HTHR27
HASN28
HLYS85
HTYR131
HHOH769
HHOH1774
site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL I 250
ChainResidue
IASP6
ITHR27
IASN28
ILYS85
ITYR131
IHOH615
IHOH1776
site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL J 250
ChainResidue
JASP6
JTHR27
JASN28
JLYS85
JTYR131
JHOH514
JHOH1778
Functional Information from PROSITE/UniProt
site_idPS00958
Number of Residues18
DetailsTRANSALDOLASE_2 Transaldolase active site. IvVKVPvTaEGLaAiKmL
ChainResidueDetails
AILE82-LEU99
site_idPS01054
Number of Residues9
DetailsTRANSALDOLASE_1 Transaldolase signature 1. GVTTNPSII
ChainResidueDetails
AGLY24-ILE32
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsActive site: {"description":"Nucleophile; Schiff-base intermediate with substrate","evidences":[{"source":"HAMAP-Rule","id":"MF_00496","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11120740","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12051943","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32519699","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2015","firstPage":"3140","lastPage":"3151","volume":"7","journal":"ChemCatChem","title":"Acid Base Catalyst Discriminates between a Fructose 6-Phosphate Aldolase and a Transaldolase.","authors":["Stellmacher L.","Sandalova T.","Leptihn S.","Schneider G.","Sprenger G.A.","Samland A.K."],"citationCrossReferences":[{"database":"DOI","id":"10.1002/cctc.201500478"}]}}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues10
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00496","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2015","firstPage":"3140","lastPage":"3151","volume":"7","journal":"ChemCatChem","title":"Acid Base Catalyst Discriminates between a Fructose 6-Phosphate Aldolase and a Transaldolase.","authors":["Stellmacher L.","Sandalova T.","Leptihn S.","Schneider G.","Sprenger G.A.","Samland A.K."],"citationCrossReferences":[{"database":"DOI","id":"10.1002/cctc.201500478"}]}}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32519699","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5ZOL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1onr
ChainResidueDetails
AASP6
ALYS85
AGLN59
site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1onr
ChainResidueDetails
JASP6
JLYS85
JGLN59
site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1onr
ChainResidueDetails
BASP6
BLYS85
BGLN59
site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1onr
ChainResidueDetails
CASP6
CLYS85
CGLN59
site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1onr
ChainResidueDetails
DASP6
DLYS85
DGLN59
site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1onr
ChainResidueDetails
EASP6
ELYS85
EGLN59
site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1onr
ChainResidueDetails
FASP6
FLYS85
FGLN59
site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1onr
ChainResidueDetails
GASP6
GLYS85
GGLN59
site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1onr
ChainResidueDetails
HASP6
HLYS85
HGLN59
site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1onr
ChainResidueDetails
IASP6
ILYS85
IGLN59

256448

PDB entries from 2026-07-15

PDB statisticsPDBj update infoContact PDBjnumon