1ADO: Aldolase

Fructose 1,6-bisphosphate aldolase from rabbit muscle. Determined by X-ray diffraction at 1.9 Å resolution. Released 24 Dec 1997.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Oryctolagus cuniculus
Chains: 4
Atoms: 14,356
Mol. weight: 157.55 kDa
Ligands: 13P
Released: 24 Dec 1997

Explore 1ADO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1ADO contains 71 α-helices and 48 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: 16 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	9-22	14
β-strand	28-32	5	1
α-helix	36-45	10
α-helix	52-63	12
α-helix	67-72	6
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
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	245-259	15
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

Chain B: 16 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	9-22	14
β-strand	28-32	5	4
α-helix	36-44	9
α-helix	52-63	12
β-strand	73-78	6	4
α-helix	80-83	4
β-strand	86	1	5
β-strand	92	1	5
α-helix	93-99	7
α-helix	102	1
β-strand	103-107	5	4
β-strand	112-114	3	6
α-helix	115	1
β-strand	122-124	3	6
α-helix	130-139	10
β-strand	144-151	8	4
α-helix	160-179	20
β-strand	183-190	8	4
α-helix	198-218	21
α-helix	223-225	3
β-strand	227-228	2	4
α-helix	245-259	15
β-strand	266-269	4	4
α-helix	276-288	13
β-strand	296-301	6	4
α-helix	303-313	11
α-helix	317-319	3
α-helix	320-337	18

Chain C: 19 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	9-22	14
β-strand	28-32	5	7
α-helix	36-44	9
α-helix	52-63	12
α-helix	67-69	3
β-strand	73-78	6	7
α-helix	80-83	4
β-strand	86	1	8
β-strand	92	1	8
α-helix	93-99	7
α-helix	102	1
β-strand	103-107	5	7
β-strand	112-114	3	9
α-helix	115	1
β-strand	122-124	3	9
α-helix	130-139	10
β-strand	144-151	8	7
α-helix	160-179	20
β-strand	183-190	8	7
α-helix	198-218	21
α-helix	223-225	3
β-strand	227-228	2	7
α-helix	245-259	15
β-strand	266-269	4	7
α-helix	276-288	13
β-strand	296-301	6	7
α-helix	303-313	11
α-helix	317-319	3
α-helix	320-337	18
α-helix	355-357	3
α-helix	360-362	3

Chain D: 20 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	9-22	14
β-strand	28-32	5	10
α-helix	36-45	10
α-helix	52-63	12
α-helix	67-69	3
β-strand	73-78	6	10
α-helix	80-83	4
β-strand	86	1	11
β-strand	92	1	11
α-helix	93-99	7
α-helix	102	1
β-strand	103-107	5	10
β-strand	112-114	3	12
β-strand	122-124	3	12
α-helix	130-139	10
β-strand	144-151	8	10
α-helix	160-179	20
β-strand	183-190	8	10
α-helix	191	1
α-helix	198-218	21
α-helix	223-225	3
β-strand	227-228	2	10
α-helix	245-259	15
β-strand	266-269	4	10
α-helix	276-287	12
β-strand	296-301	6	10
α-helix	303-313	11
α-helix	317-319	3
α-helix	320-337	18
α-helix	350-352	3
α-helix	356-358	3
α-helix	360-362	3

Molecules and chains

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

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

>1ADO_1 ALDOLASE (chains A, B, C, D)
PHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQ
LLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNG
ETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQN
GIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACT
QKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFS
YGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTSSGQAGAAASESLFISN
HAY

Ligands and cofactors

ID	Name	Formula	Copies
13P	1,3-dihydroxyacetonephosphate	C3 H7 O6 P	2

Water and common crystallization additives (SO4) are not listed.

Primary citation

Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase. Blom, N., Sygusch, J. Nat Struct Biol (1997) 4:36-39. DOI 10.1038/nsb0197-36 · 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…
3DFO 1.94 Å, Dihydroxyacetone phosphate Schiff base and enamine intermediates in D33N mutant…
3DFT 1.94 Å, Phosphate ions in D33S mutant fructose-1,6-bisphosphate aldolase from rabbit muscle

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