5KY6: Human muscle fructose-1,6-bisphosphate aldolase

Human muscle fructose-1,6-bisphosphate aldolase. Determined by X-ray diffraction at 1.94 Å resolution. Released 28 Jun 2017.

Method: X-ray diffraction
Resolution: 1.94 Å
Organism: Homo sapiens
Chains: 4
Atoms: 10,664
Mol. weight: 157.36 kDa
Released: 28 Jun 2017

Explore 5KY6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5KY6 contains 74 α-helices and 56 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: 19 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	9-22	14
β-strand	28-32	5	1
α-helix	36-39	4
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
α-helix	182	1
β-strand	183-190	8	1
α-helix	191	1
α-helix	198-218	21
α-helix	223-225	3
β-strand	227-228	2	1
α-helix	230	1
β-strand	231	1	4
α-helix	232-233	2
α-helix	245-257	13
β-strand	266-269	4	1
β-strand	270	1	4
α-helix	276-288	13
β-strand	296-301	6	1
α-helix	303-306	4
α-helix	321-337	17

Chain B: 18 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	9-22	14
β-strand	28-32	5	5
α-helix	36-39	4
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
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	160-179	20
β-strand	183-190	8	5
α-helix	198-218	21
α-helix	223-225	3
β-strand	227-228	2	5
α-helix	230	1
β-strand	231	1	8
α-helix	232-233	2
α-helix	245-257	13
β-strand	266-269	4	5
β-strand	270	1	8
α-helix	276-288	13
β-strand	296-301	6	5
α-helix	303-306	4
α-helix	320-337	18
α-helix	356-358	3
α-helix	360-362	3

Chain C: 19 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	9-22	14
β-strand	28-32	5	9
α-helix	36-39	4
α-helix	52-63	12
α-helix	67-69	3
β-strand	73-78	6	9
α-helix	80-83	4
β-strand	86	1	10
β-strand	92	1	10
α-helix	93-99	7
α-helix	102	1
β-strand	103-107	5	9
β-strand	112-114	3	11
α-helix	115	1
β-strand	122-124	3	11
α-helix	130-139	10
β-strand	144-151	8	9
α-helix	160-179	20
β-strand	183-190	8	9
α-helix	198-218	21
α-helix	223-225	3
β-strand	227-228	2	9
α-helix	230	1
β-strand	231	1	12
α-helix	232	1
α-helix	245-259	15
β-strand	266-269	4	9
β-strand	270	1	12
α-helix	276-288	13
β-strand	296-301	6	9
α-helix	303-306	4
α-helix	320-337	18
α-helix	360-362	3

Chain D: 18 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	9-22	14
β-strand	28-32	5	13
α-helix	36-39	4
α-helix	52-63	12
α-helix	67-69	3
β-strand	73-78	6	13
α-helix	80-83	4
β-strand	86	1	14
β-strand	92	1	14
α-helix	93-99	7
α-helix	102	1
β-strand	103-107	5	13
β-strand	112-114	3	15
β-strand	122-124	3	15
α-helix	130-139	10
β-strand	144-151	8	13
α-helix	160-179	20
β-strand	183-190	8	13
α-helix	191	1
α-helix	198-218	21
α-helix	223-225	3
β-strand	227-228	2	13
α-helix	230	1
β-strand	231	1	16
α-helix	232	1
α-helix	245-259	15
β-strand	266-269	4	13
β-strand	270	1	16
α-helix	276-288	13
β-strand	296-301	6	13
α-helix	303-306	4
α-helix	320-337	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fructose-bisphosphate aldolase A	A, B, C, D	protein	363	Homo sapiens	P04075 (AlphaFold model)

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

>5KY6_1 Fructose-bisphosphate aldolase A (chains A, B, C, D)
PYQYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQ
LLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNG
ETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQN
GIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACT
QKFSHEEIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFS
YGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFVSN
HAY

Primary citation

Crystal structure of human muscle aldolase. Wisniewski, J., Barciszewski, J., Jaskolski, M. et al. To be published.

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
6XMH 1.95 Å, Human aldolase A wild type
1ALD 2.0 Å, Activity and specificity of human aldolases
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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