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- PDB-9o6o: Structure of SigLec-10 in complex with 2,6-Sialyllactose -

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Basic information

Entry
Database: PDB / ID: 9o6o
TitleStructure of SigLec-10 in complex with 2,6-Sialyllactose
ComponentsSialic acid-binding Ig-like lectin 10
KeywordsIMMUNE SYSTEM / Siglec / Receptor / Sialic Acid
Function / homology
Function and homology information


negative regulation of inflammatory response to wounding / sialic acid binding / phosphatase binding / SH2 domain binding / adaptive immune response / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / actin cytoskeleton / carbohydrate binding / cell adhesion / innate immune response ...negative regulation of inflammatory response to wounding / sialic acid binding / phosphatase binding / SH2 domain binding / adaptive immune response / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / actin cytoskeleton / carbohydrate binding / cell adhesion / innate immune response / extracellular region / plasma membrane / cytosol
Similarity search - Function
SIGLEC family-like protein 1 C-terminal domain / : / Immunoglobulin domain / Immunoglobulin I-set / Immunoglobulin I-set domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Immunoglobulin V-set domain / Immunoglobulin V-set domain / Immunoglobulin/major histocompatibility complex, conserved site ...SIGLEC family-like protein 1 C-terminal domain / : / Immunoglobulin domain / Immunoglobulin I-set / Immunoglobulin I-set domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Immunoglobulin V-set domain / Immunoglobulin V-set domain / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
N-acetyl-alpha-neuraminic acid / Sialic acid-binding Ig-like lectin 10
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å
AuthorsMedina, E. / Ming, Q. / Tran, T.H. / Luca, V.C.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)1R35GM133482 United States
CitationJournal: Structure / Year: 2026
Title: Structural basis for sialoglycan recognition by the immune inhibitory receptor Siglec-10.
Authors: Medina, E. / Mason, C. / Tran, T.H. / Julia, E.P. / Ming, Q. / Taibi, L.M. / Hwu, P. / Maute, R.L. / Burg, J.S. / Luca, V.C.
History
DepositionApr 14, 2025Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 25, 2026Provider: repository / Type: Initial release
Revision 1.1Sep 9, 2026Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
B: Sialic acid-binding Ig-like lectin 10
A: Sialic acid-binding Ig-like lectin 10
D: Sialic acid-binding Ig-like lectin 10
hetero molecules


Theoretical massNumber of molelcules
Total (without water)76,76817
Polymers74,1293
Non-polymers2,63814
Water30617
1
B: Sialic acid-binding Ig-like lectin 10
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,2996
Polymers24,7101
Non-polymers5905
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
A: Sialic acid-binding Ig-like lectin 10
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,8826
Polymers24,7101
Non-polymers1,1725
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
D: Sialic acid-binding Ig-like lectin 10
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,5875
Polymers24,7101
Non-polymers8774
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)83.188, 83.188, 484.668
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number179
Space group name H-MP6522

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Components

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Protein , 1 types, 3 molecules BAD

#1: Protein Sialic acid-binding Ig-like lectin 10 / Siglec-10 / Siglec-like protein 2


Mass: 24709.758 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SIGLEC10, SLG2, UNQ477/PRO940 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q96LC7

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Sugars , 4 types, 5 molecules

#2: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 1 / Source method: obtained synthetically
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}LINUCSPDB-CARE
#3: Polysaccharide N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose


Type: oligosaccharide / Mass: 471.411 Da / Num. of mol.: 1 / Source method: isolated from a natural source
DescriptorTypeProgram
DNeup5Aca2-6DGalpb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[a2112h-1b_1-5][Aad21122h-2a_2-6_5*NCC/3=O]/1-2/a6-b2WURCSPDB2Glycan 1.1.0
[][b-D-Galp]{[(6+2)][a-D-Neup5Ac]{}}LINUCSPDB-CARE
#5: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H15NO6 / Feature type: SUBJECT OF INVESTIGATION
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#6: Sugar ChemComp-SIA / N-acetyl-alpha-neuraminic acid / N-acetylneuraminic acid / sialic acid / alpha-sialic acid / O-SIALIC ACID


Type: D-saccharide, alpha linking / Mass: 309.270 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C11H19NO9 / Feature type: SUBJECT OF INVESTIGATION
IdentifierTypeProgram
DNeup5AcaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-a-D-neuraminic acidCOMMON NAMEGMML 1.0
a-D-Neup5AcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
Neu5AcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 2 types, 26 molecules

#4: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: C3H8O3 / Feature type: SUBJECT OF INVESTIGATION
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 17 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.27 Å3/Da / Density % sol: 62.33 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, hanging drop
Details: 0.085 M Sodium Citrate pH 5.1, 0.17 M Ammonium Acetate, 15% v/v Glycerol, and 29% w/v PEG 4000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL12-1 / Wavelength: 0.97946 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Mar 25, 2024
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97946 Å / Relative weight: 1
ReflectionResolution: 2.7→48.11 Å / Num. obs: 28605 / % possible obs: 99.8 % / Redundancy: 16.6 % / CC1/2: 0.996 / Rmerge(I) obs: 0.192 / Rpim(I) all: 0.049 / Rrim(I) all: 0.199 / Χ2: 1.12 / Net I/σ(I): 12.6 / Num. measured all: 474434
Reflection shellResolution: 2.7→2.83 Å / % possible obs: 98.7 % / Redundancy: 13.8 % / Rmerge(I) obs: 0.59 / Num. measured all: 49842 / Num. unique obs: 3614 / CC1/2: 0.84 / Rpim(I) all: 0.16 / Rrim(I) all: 0.612 / Χ2: 0.4 / Net I/σ(I) obs: 3.1

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Processing

Software
NameVersionClassification
REFMAC5.8.0425refinement
XSCALEdata scaling
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.7→39.37 Å / Cor.coef. Fo:Fc: 0.942 / Cor.coef. Fo:Fc free: 0.908 / SU B: 15.063 / SU ML: 0.29 / Cross valid method: THROUGHOUT / ESU R: 0.603 / ESU R Free: 0.34 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
RfactorNum. reflection% reflectionSelection details
Rfree0.27626 1444 5.1 %RANDOM
Rwork0.22079 ---
obs0.22356 27085 99.56 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 78.497 Å2
Baniso -1Baniso -2Baniso -3
1-2.02 Å21.01 Å20 Å2
2--2.02 Å2-0 Å2
3----6.54 Å2
Refinement stepCycle: 1 / Resolution: 2.7→39.37 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5206 0 174 17 5397
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.0125541
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.7631.8257549
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.0265653
X-RAY DIFFRACTIONr_dihedral_angle_2_deg5.793545
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.19510815
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.1550.2830
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.024294
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it6.7257.5412621
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it9.88913.5383271
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it8.428.0252920
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined15.69291.817808
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.704→2.849 Å / Total num. of bins used: 10
RfactorNum. reflection% reflection
Rfree0.484 196 -
Rwork0.36 3744 -
obs--97.72 %

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