9UBR: Human Galectin-10 with iTrimbody

CryoEM structure of human Galectin-10 with iTrimbody. Determined by electron microscopy at 2.62 Å resolution. Released 11 Feb 2026.

Method: Electron microscopy
Resolution: 2.62 Å
Organisms: synthetic construct, Thermotoga maritima MSB8, Homo sapiens
Chains: 18
Atoms: 23,871
Mol. weight: 340.82 kDa
Released: 11 Feb 2026

Explore 9UBR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9UBR contains 108 α-helices and 228 β-strands across 18 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: 13 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	9-16	8
α-helix	23-35	13
α-helix	37-39	3
α-helix	40-72	33
β-strand	74-78	5	1
α-helix	83-95	13
β-strand	100-104	5	1
α-helix	110-116	7
α-helix	118-122	5
β-strand	126-130	5	1
α-helix	135-142	8
β-strand	148-150	3	1
α-helix	156-165	10
β-strand	168-170	3	1
β-strand	172-173	2	2
α-helix	176-184	9
β-strand	189-192	4	2
α-helix	195-205	11
β-strand	214-217	4	2
β-strand	218	1	1
α-helix	223-232	10
β-strand	237-239	3	1
α-helix	248-262	15

Chain B: 14 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	9-16	8
α-helix	23-35	13
α-helix	37-39	3
α-helix	40-72	33
β-strand	74-78	5	3
α-helix	83-94	12
β-strand	100-104	5	3
α-helix	110-116	7
α-helix	118-121	4
β-strand	126-130	5	3
α-helix	135-143	9
β-strand	148-150	3	3
α-helix	156-164	9
β-strand	168-170	3	3
β-strand	172-173	2	4
α-helix	176-183	8
β-strand	189-190	2	5
β-strand	191-192	2	4
α-helix	195-198	4
α-helix	200-207	8
β-strand	214-215	2	5
β-strand	218	1	3
α-helix	223-231	9
β-strand	237-239	3	3
α-helix	248-264	17

Chain C: 14 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	9-16	8
α-helix	23-35	13
α-helix	37-39	3
α-helix	40-72	33
β-strand	74-78	5	6
α-helix	83-95	13
β-strand	100-104	5	6
α-helix	110-116	7
α-helix	118-121	4
β-strand	126-130	5	6
α-helix	135-143	9
β-strand	148-150	3	6
α-helix	156-165	10
β-strand	168-170	3	6
β-strand	172-173	2	7
α-helix	176-183	8
β-strand	189-192	4	7
α-helix	195-198	4
α-helix	200-206	7
β-strand	214-217	4	7
β-strand	218	1	6
α-helix	223-230	8
β-strand	237-239	3	6
α-helix	248-264	17

Chain D: 13 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
α-helix	23-35	13
α-helix	37-39	3
α-helix	40-72	33
β-strand	75-78	4	8
α-helix	83-94	12
β-strand	100-104	5	8
α-helix	110-116	7
α-helix	118-122	5
β-strand	126-130	5	8
α-helix	135-142	8
β-strand	148-150	3	8
α-helix	156-165	10
β-strand	168-170	3	8
β-strand	172-173	2	9
α-helix	176-184	9
β-strand	189-190	2	10
β-strand	191-192	2	9
α-helix	195-207	13
β-strand	214-215	2	10
β-strand	218	1	8
α-helix	226-232	7
β-strand	238-239	2	8
α-helix	248-263	16

Chain E: 13 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	9-16	8
α-helix	23-35	13
α-helix	37-39	3
α-helix	40-72	33
β-strand	74-78	5	11
α-helix	83-95	13
β-strand	100-104	5	11
α-helix	110-115	6
α-helix	118-121	4
β-strand	126-130	5	11
α-helix	135-142	8
β-strand	148-150	3	11
α-helix	156-165	10
β-strand	168-170	3	11
β-strand	172-173	2	12
α-helix	176-183	8
β-strand	189-190	2	13
β-strand	191-192	2	12
α-helix	195-205	11
β-strand	214-215	2	13
β-strand	218	1	11
α-helix	223-232	10
β-strand	237-239	3	11
α-helix	248-262	15

Chain F: 13 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	9-16	8
α-helix	23-35	13
α-helix	37-39	3
α-helix	40-72	33
β-strand	74-78	5	14
α-helix	83-95	13
β-strand	100-104	5	14
α-helix	110-116	7
α-helix	118-121	4
β-strand	126-130	5	14
α-helix	135-143	9
β-strand	148-150	3	14
α-helix	156-165	10
β-strand	168-170	3	14
β-strand	172-173	2	15
α-helix	176-184	9
β-strand	189-192	4	15
α-helix	195-206	12
β-strand	214-217	4	15
β-strand	218	1	14
α-helix	223-232	10
β-strand	237-239	3	14
α-helix	248-264	17

Chain G: 3 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	6-9	4	16
β-strand	12	1	17
α-helix	14	1
β-strand	15	1	18
β-strand	20-26	7	16
β-strand	32-38	7	17
β-strand	45-51	7	17
β-strand	56-58	3	17
β-strand	66-71	6	16
β-strand	76-81	6	16
α-helix	86-88	3
β-strand	90-97	8	17
α-helix	104-106	3
β-strand	109	1	17
β-strand	111	1	16
β-strand	114-116	3	17
β-strand	119	1	18

Chain H: 3 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	6-9	4	19
β-strand	12	1	20
α-helix	14	1
β-strand	15	1	21
β-strand	20-21	2	19
β-strand	23-26	4	19
β-strand	32-38	7	20
β-strand	44-51	8	20
β-strand	56-58	3	20
β-strand	63	1	19
β-strand	66-71	6	19
β-strand	76-81	6	19
α-helix	86-88	3
β-strand	90-97	8	20
α-helix	104-106	3
β-strand	109	1	20
β-strand	111	1	19
β-strand	114-116	3	20
β-strand	119	1	21

10 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
PrAC-5350A,2-dehydro-3-deoxyphosphogluconate aldolase/4-hydroxy-2-oxoglutarate aldolase	A, B, C, D, E, F	protein	260	synthetic construct, Thermotoga maritima MSB8	Q9WXS1 (AlphaFold model)
hGal10-nanobody	G, H, I, J, K, L	protein	118	synthetic construct
Galectin-10	M, N, O, P, Q, R	protein	140	Homo sapiens	Q05315 (AlphaFold model)

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

>9UBR_1 PrAC-5350A,2-dehydro-3-deoxyphosphogluconate aldolase/4-hydroxy-2-oxoglutarate aldolase (chains A, B, C, D, E, F)
QANAFAQILNMPNLTEEQRNGFIQSLKDDPSVSKEILAEAKKLNEHQAAKAEEAARKMEE
LFKKHKIVAVLRANSVEEAIEKAVAVFAGGVHLIEITFTVPDADTVIKALSVLKEKGAII
GAGTVTSVEQCRKAVESGAEFIVSPHLDEEISQFCKEKGVFYMPGVMTPTELVKAMKLGH
TILKLFPGEVVGPQFVKAMKGPFPNVKFVPTGGVNLDNVCEWFKAGVLAVGVGSALVKGT
PDEVREKAKAFVEKIRGCTE

Sequence of entity 2 (G, H, I, J, K, L), FASTA

>9UBR_2 hGal10-nanobody (chains G, H, I, J, K, L)
EVQLLESGGGSVQAGGSLRLSCTASGYTYSVAWFRQAPGNEREGVAVISNYGATTYSDSV
KGRFTISRDNAKNAVSLQMNSLKSEDTAMYYCAAGSAFSLSPGRFPYWGQGTQVTVSS

Sequence of entity 3 (M, N, O, P, Q, R), FASTA

>9UBR_3 Galectin-10 (chains M, N, O, P, Q, R)
SLLPVPYTEAASLSTGSTVTIKGRPLACFLNEPYLQVDFHTEMKEESDIVFHFQVCFGRR
VVMNSREYGAWKQQVESKNMPFQDGQEFELSISVLPDKYQVMVNGQSSYTFDHRIKPEAV
KMVQVWRDISLTKFNVSYLK

Primary citation

CryoEM structure of human Galectin-10 with iTrimbody. Song, J.Y., Wang, W. To be published.

Other PDB entries of the same protein (UniProt Q9WXS1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1WA3 1.9 Å, Mechanism of the Class I KDPG aldolase
9UAQ 2.29 Å, CryoEM structure of GFP-like protein from Aequorea coerulescens with Trimbody
1VLW 2.3 Å, Crystal structure of 2-dehydro-3-deoxyphosphogluconate aldolase/4-hydroxy-2-oxoglutarate…
9UCL 2.43 Å, CryoEM structure of IgV domain of human Nectin-4 with Trimbody
9XOU 2.5 Å, CryoEM structure of LacY with Trimbody
8SZZ 2.9 Å, CryoEM Structure of Computationally Designed Nanocage O32-ZL4
8TVB 2.9 Å, Ghanaian virus fusion glycoprotein (GhV F)
8TYC 3.3 Å, Lassa GPC (strain Josiah) bound to rabbit polyclonal base-targeting antibody Base-1
8E01 3.4 Å, Structure of engineered nano-cage fusion protein
8JGC 3.44 Å, Cryo-EM structure of Mi3 fused with LOV2
8JGA 3.68 Å, Cryo-EM structure of Mi3 fused with FKBP
7B3Y 3.7 Å, Structure of a nanoparticle for a COVID-19 vaccine candidate

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