3DFS: Fructose-bisphosphate aldolase A

Dihydroxyacetone phosphate Schiff base intermediate in D33S mutant fructose-1,6-bisphosphate aldolase from rabbit muscle. Determined by X-ray diffraction at 2.03 Å resolution. Released 28 Apr 2009.

Method: X-ray diffraction
Resolution: 2.03 Å
Organism: Oryctolagus cuniculus
Chains: 4
Atoms: 12,915
Mol. weight: 157.62 kDa
Ligands: 13P
Released: 28 Apr 2009

Explore 3DFS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3DFS contains 67 α-helices and 52 β-strands across 4 chains. 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

Element	Residues	Length	Sheet
α-helix	9-22	14
β-strand	28-32	5	1
α-helix	36-44	9
α-helix	52-63	12
α-helix	67-69	3
β-strand	73-78	6	1
α-helix	80-83	4
β-strand	86	1	2
β-strand	92	1	2
α-helix	93-99	7
α-helix	102	1
β-strand	103-107	5	1
β-strand	112-114	3	3
β-strand	122-124	3	3
α-helix	130-139	10
β-strand	144-151	8	1
β-strand	154	1	4
β-strand	157	1	4
α-helix	160-179	20
β-strand	183-190	8	1
α-helix	198-218	21
α-helix	223-225	3
β-strand	227-228	2	1
α-helix	245-257	13
β-strand	266-269	4	1
α-helix	276-288	13
β-strand	296-301	6	1
α-helix	303-313	11
α-helix	317-319	3
α-helix	320-337	18
α-helix	360-362	3

Chain B: 17 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	9-22	14
β-strand	28-32	5	5
α-helix	36-44	9
α-helix	52-63	12
α-helix	67-69	3
β-strand	73-78	6	5
α-helix	80-83	4
β-strand	86	1	6
β-strand	92	1	6
α-helix	93-99	7
α-helix	102	1
β-strand	103-107	5	5
β-strand	112-114	3	7
β-strand	122-124	3	7
α-helix	130-139	10
β-strand	144-151	8	5
α-helix	160-178	19
β-strand	183-190	8	5
α-helix	198-218	21
α-helix	223-225	3
β-strand	227-228	2	5
α-helix	245-257	13
β-strand	266-269	4	5
α-helix	276-288	13
β-strand	296-301	6	5
α-helix	303-313	11
α-helix	317-319	3
α-helix	320-337	18
α-helix	360-362	3

Chain C: 16 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	9-22	14
β-strand	28-32	5	8
α-helix	36-44	9
α-helix	52-63	12
α-helix	67-69	3
β-strand	73-78	6	8
α-helix	80-83	4
β-strand	86	1	9
β-strand	92	1	9
α-helix	93-99	7
α-helix	102	1
β-strand	103-107	5	8
β-strand	112-114	3	10
β-strand	122-124	3	10
α-helix	130-139	10
β-strand	144-151	8	8
α-helix	160-179	20
β-strand	183-190	8	8
α-helix	198-218	21
α-helix	223-225	3
β-strand	227-228	2	8
α-helix	245-257	13
β-strand	266-269	4	8
α-helix	276-288	13
β-strand	296-301	6	8
α-helix	303-313	11
α-helix	317-319	3
α-helix	320-337	18
β-strand	343	1	11
β-strand	346	1	11

Chain D: 17 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	9-22	14
β-strand	28-32	5	12
α-helix	36-44	9
α-helix	52-63	12
α-helix	67-69	3
β-strand	73-78	6	12
α-helix	80-83	4
β-strand	86	1	13
β-strand	92	1	13
α-helix	93-99	7
α-helix	102	1
β-strand	103-107	5	12
β-strand	112-114	3	14
β-strand	122-124	3	14
α-helix	130-139	10
β-strand	144-151	8	12
α-helix	160-178	19
β-strand	183-190	8	12
α-helix	198-218	21
α-helix	223-225	3
β-strand	227-228	2	12
α-helix	230-232	3
α-helix	245-257	13
β-strand	266-269	4	12
α-helix	276-288	13
β-strand	296-301	6	12
α-helix	303-313	11
α-helix	317-319	3
α-helix	320-337	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fructose-bisphosphate aldolase A	A, B, C, D	protein	363	Oryctolagus cuniculus	P00883 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>3DFS_1 Fructose-bisphosphate aldolase A (chains A, B, C, D)
PHSHPALTPEQKKELSDIAHRIVAPGKGILAASESTGSIAKRLQSIGTENTEENRRFYRQ
LLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNG
ETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQN
GIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACT
QKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFS
YGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFISN
HAY

Ligands and cofactors

ID	Name	Formula	Copies
13P	1,3-dihydroxyacetonephosphate	C3 H7 O6 P	4

Primary citation

Charge stabilization and entropy reduction of central lysine residues in fructose-bisphosphate aldolase. St-Jean, M., Blonski, C., Sygusch, J. Biochemistry (2009) 48:4528-4537. DOI 10.1021/bi8021558 · PubMed

Other PDB entries of the same protein (UniProt P00883 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5TLE 1.58 Å, Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor…
3BV4 1.7 Å, Crystal structure of a rabbit muscle fructose-1,6-bisphosphate aldolase A dimer variant
1ZAI 1.76 Å, Fructose-1,6-bisphosphate Schiff base intermediate in FBP aldolase from rabbit muscle
1ZAH 1.8 Å, Fructose-1,6-bisphosphate aldolase from rabbit muscle
3DFQ 1.82 Å, D33S mutant fructose-1,6-bisphosphate aldolase from rabbit muscle
5F4X 1.84 Å, Fructose-1,6-bisphosphate aldolase K229M mutant from rabbit muscle
3DFN 1.86 Å, D33N mutant fructose-1,6-bisphosphate aldolase from rabbit muscle
2QUT 1.88 Å, Dihydroxyacetone phosphate enamine intermediate in fructose-1,6-bisphosphate aldolase…
1ZAJ 1.89 Å, Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with…
1ZAL 1.89 Å, Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with partially…
1ADO 1.9 Å, Fructose 1,6-bisphosphate aldolase from rabbit muscle
3DFO 1.94 Å, Dihydroxyacetone phosphate Schiff base and enamine intermediates in D33N mutant…

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