1ALD: Activity and specificity of human aldolases

Activity and specificity of human aldolases. Determined by X-ray diffraction at 2.0 Å resolution. Released 15 Jan 1992.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,763
Mol. weight: 39.34 kDa
Released: 15 Jan 1992

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

Secondary structure: helices and β-sheets

1ALD contains 16 α-helices and 12 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: 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	82-84	3
β-strand	86	1	2
β-strand	92	1	2
α-helix	93-99	7
β-strand	103-107	5	1
β-strand	112-114	3	3
α-helix	115	1
β-strand	122-124	3	3
α-helix	130-139	10
β-strand	144-151	8	1
α-helix	160-178	19
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

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Aldolase a	A	protein	363	Homo sapiens	P04075 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1ALD_1 ALDOLASE A (chains A)
PYQYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQ
LLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNG
ETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQN
GIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACT
QKFSHEEIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFS
YGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFVSN
HAY

Primary citation

Activity and specificity of human aldolases. Gamblin, S.J., Davies, G.J., Grimes, J.M. et al. J Mol Biol (1991) 219:573-576. DOI 10.1016/0022-2836(91)90650-U · PubMed

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

6XML 1.88 Å, Human aldolase A I98C
5KY6 1.94 Å, Human muscle fructose-1,6-bisphosphate aldolase
6XMH 1.95 Å, Human aldolase A wild type
2ALD 2.1 Å, Human muscle aldolase
6XMM 2.11 Å, Human aldolase A I98S
6XMO 2.6 Å, Human aldolase A I98F
4ALD 2.8 Å, Human muscle fructose 1,6-bisphosphate aldolase complexed with fructose 1,6-bisphosphate

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