2QUU: Fructose-bisphosphate aldolase A

Dihydroxyacetone phosphate Schiff base intermediate in mutant fructose-1,6-bisphosphate aldolase from rabbit muscle. Determined by X-ray diffraction at 1.98 Å resolution. Released 28 Aug 2007.

Method: X-ray diffraction
Resolution: 1.98 Å
Organism: Oryctolagus cuniculus
Chains: 4
Atoms: 13,086
Mol. weight: 157.74 kDa
Ligands: 13P
Released: 28 Aug 2007

Explore 2QUU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2QUU contains 69 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: 17 helices, 12 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
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	4
α-helix	36-44	9
α-helix	52-63	12
α-helix	67-72	6
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
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	245-257	13
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
α-helix	360-362	3

Chain C: 17 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	9-22	14
β-strand	28-32	5	7
α-helix	40-44	5
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
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	230-232	3
α-helix	245-257	13
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

Chain D: 18 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	9-22	14
β-strand	28-32	5	10
α-helix	36-44	9
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	160-178	19
β-strand	183-190	8	10
α-helix	198-218	21
α-helix	223-225	3
β-strand	227-228	2	10
α-helix	230-232	3
α-helix	245-257	13
β-strand	266-269	4	10
α-helix	276-288	13
β-strand	296-301	6	10
α-helix	303-313	11
α-helix	317-319	3
α-helix	320-337	18
α-helix	350-353	4

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

>2QUU_1 Fructose-bisphosphate aldolase A (chains A, B, C, D)
PHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQ
LLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNG
ETTTQGLDGLSERCAQYKKDGADFAMWRCVLKIGEHTPSALAIMENANVLARYASICQQN
GIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACT
QKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFS
YGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFISN
HAY

Ligands and cofactors

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

Primary citation

Stereospecific proton transfer by a mobile catalyst in mammalian fructose-1,6-bisphosphate aldolase. St-Jean, M., Sygusch, J. J Biol Chem (2007) 282:31028-31037. DOI 10.1074/jbc.M704968200 · 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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