6XMM: Human aldolase A I98S

Human aldolase A I98S. Determined by X-ray diffraction at 2.11 Å resolution. Released 7 Jul 2021.

Method: X-ray diffraction
Resolution: 2.11 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,477
Mol. weight: 79.82 kDa
Ligands: PO4
Released: 7 Jul 2021

Explore 6XMM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6XMM contains 33 α-helices and 26 β-strands across 2 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	10-23	14
β-strand	29-33	5	1
α-helix	39-45	7
α-helix	53-64	12
β-strand	74-79	6	1
α-helix	81-84	4
β-strand	87	1	2
β-strand	93	1	2
α-helix	94-100	7
β-strand	104-108	5	1
β-strand	113-115	3	3
α-helix	116	1
β-strand	123-125	3	3
α-helix	131-140	10
β-strand	145-152	8	1
α-helix	161-180	20
β-strand	184-191	8	1
α-helix	199-219	21
α-helix	224-226	3
β-strand	228-229	2	1
α-helix	231-233	3
α-helix	246-258	13
β-strand	267-270	4	1
α-helix	277-289	13
β-strand	297-302	6	1
α-helix	304-314	11
α-helix	318-320	3
α-helix	321-338	18

Chain B: 17 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	10-23	14
β-strand	29-33	5	4
α-helix	37-44	8
α-helix	45-47	3
α-helix	53-64	12
α-helix	71-73	3
β-strand	74-79	6	4
α-helix	81-84	4
β-strand	87	1	5
β-strand	93	1	5
α-helix	94-99	6
β-strand	104-108	5	4
β-strand	113-115	3	6
β-strand	123-125	3	6
α-helix	131-140	10
β-strand	143-152	10	4
β-strand	155	1	7
β-strand	158	1	7
α-helix	161-180	20
β-strand	184-191	8	4
α-helix	192	1
α-helix	199-219	21
β-strand	228-229	2	4
α-helix	232-234	3
α-helix	246-258	13
β-strand	267-270	4	4
α-helix	279-288	10
β-strand	297-302	6	4
α-helix	304-314	11
α-helix	318-320	3
α-helix	321-338	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fructose-bisphosphate aldolase A	A, B	protein	364	Homo sapiens	P04075 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6XMM_1 Fructose-bisphosphate aldolase A (chains A, B)
MPYQYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYR
QLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVSKSKGGVVGIKVDKGVVPLAGTN
GETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQ
NGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHAC
TQKFSHEEIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTF
SYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFVS
NHAY

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	4

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

Primary citation

Substitutions at a rheostat position in human aldolase A cause a shift in the conformational population. Fenton, K.D., Meneely, K.M., Wu, T. et al. Protein Sci (2022) 31:357-370. DOI 10.1002/pro.4222 · 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
1ALD 2.0 Å, Activity and specificity of human aldolases
2ALD 2.1 Å, Human muscle aldolase
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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