4ALD: Human muscle fructose 1,6-bisphosphate aldolase

Human muscle fructose 1,6-bisphosphate aldolase complexed with fructose 1,6-bisphosphate. Determined by X-ray diffraction at 2.8 Å resolution. Released 2 Mar 1999.

Method
X-ray diffraction
Resolution
2.8 Å
Organism
Homo sapiens
Chains
1
Atoms
2,783
Mol. weight
39.68 kDa
Ligands
2FP
Released
2 Mar 1999

Explore 4ALD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ALD contains 17 α-helices and 14 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 17 helices, 14 β-strands

ElementResiduesLengthSheet
α-helix9-2214
β-strand28-3251
α-helix36-4510
α-helix52-6312
β-strand73-7861
α-helix791
α-helix80-845
β-strand8612
β-strand9212
α-helix93-997
β-strand103-10751
β-strand112-11433
β-strand122-12433
α-helix130-13910
β-strand144-15181
β-strand15414
β-strand15714
α-helix160-17819
β-strand183-19081
α-helix1911
α-helix198-21821
α-helix223-2253
β-strand227-22821
α-helix231-2333
α-helix245-25713
β-strand266-26941
α-helix276-28813
β-strand296-30161
α-helix303-31311
α-helix317-3193
α-helix320-33718

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Fructose-bisphosphate aldolaseAprotein363Homo sapiensP04075 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4ALD_1 FRUCTOSE-BISPHOSPHATE ALDOLASE (chains A)
PYQYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQ
LLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNG
ETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQN
GIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACT
QKFSHEEIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFS
YGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFVSN
HAY

Ligands and cofactors

IDNameFormulaCopies
2FP1,6-fructose diphosphate (linear form)C6 H14 O12 P21

Primary citation

Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications. Dalby, A., Dauter, Z., Littlechild, J.A. Protein Sci (1999) 8:291-297. PubMed

Other PDB entries of the same protein (UniProt P04075 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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4ALD is part of these collections:

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