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- PDB-2zg2: Crystal Structure of Two N-terminal Domains of Native Siglec-5 -

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Basic information

Entry
Database: PDB / ID: 2zg2
TitleCrystal Structure of Two N-terminal Domains of Native Siglec-5
ComponentsSialic acid-binding Ig-like lectin 5
KeywordsIMMUNE SYSTEM/CARBOHYDRATE BINDING PROTEIN / Siglec-5 inhibitory receptor / two-domain structure / V-set / C2-set / Ig-like domain / sialic acid / Cell adhesion / Glycoprotein / Immunoglobulin domain / Lectin / Membrane / Polymorphism / Transmembrane / IMMUNE SYSTEM-CARBOHYDRATE BINDING PROTEIN COMPLEX
Function / homology
Function and homology information


sialic acid binding / tertiary granule membrane / ficolin-1-rich granule membrane / secretory granule membrane / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / carbohydrate binding / cell adhesion / Neutrophil degranulation / plasma membrane
Similarity search - Function
Immunoglobulin domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Immunoglobulin V-set domain / Immunoglobulin V-set domain / Immunoglobulin subtype / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain ...Immunoglobulin domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Immunoglobulin V-set domain / Immunoglobulin V-set domain / Immunoglobulin subtype / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Sialic acid-binding Ig-like lectin 5
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Molecular Replacement, SAD / Resolution: 2.85 Å
AuthorsZhuravleva, M.A. / Sun, P.D.
CitationJournal: J.Mol.Biol. / Year: 2008
Title: Structural implications of Siglec-5-mediated sialoglycan recognition
Authors: Zhuravleva, M.A. / Trandem, K. / Sun, P.D.
History
DepositionJan 17, 2008Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Feb 5, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Oct 11, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.3Nov 1, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Sialic acid-binding Ig-like lectin 5


Theoretical massNumber of molelcules
Total (without water)24,5331
Polymers24,5331
Non-polymers00
Water55831
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)93.146, 93.146, 205.805
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number155
Space group name H-MH32
Components on special symmetry positions
IDModelComponents
11A-269-

HOH

21A-270-

HOH

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Components

#1: Antibody Sialic acid-binding Ig-like lectin 5 / Siglec-5 / Obesity-binding protein 2 / OB-binding protein 2 / OB-BP2 / CD33 antigen-like 2 / CD170 antigen


Mass: 24532.592 Da / Num. of mol.: 1
Fragment: N-terminal V-set and C2-set domain, UNP residues 20-233
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SIGLEC5 / Plasmid: pET30a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: O15389
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 31 / Source method: isolated from a natural source / Formula: H2O

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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: 3.5 Å3/Da / Density % sol: 64.88 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8
Details: 20% MPEG 550, 0.1M TRIS, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Mar 9, 2006
RadiationMonochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.75→50 Å / Num. obs: 9235 / Observed criterion σ(I): -3 / Redundancy: 6.9 % / Rsym value: 0.067 / Net I/σ(I): 23
Reflection shellHighest resolution: 2.75 Å / Rsym value: 0.47

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Processing

Software
NameClassification
HKL-2000data collection
BRUTEmodel building
CNSrefinement
HKL-2000data reduction
SCALEPACKdata scaling
BRUTEphasing
RefinementMethod to determine structure: Molecular Replacement, SAD
Starting model: PDB ENTRY 1O7S and 1VCA

1o7s

1vca


Resolution: 2.85→30 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.291 421 -RANDOM
Rwork0.248 ---
all-8324 --
obs-7951 95.5 %-
Displacement parametersBiso mean: 88 Å2
Refinement stepCycle: LAST / Resolution: 2.85→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1697 0 0 31 1728
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.008
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg1.46
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it1.4761.5
X-RAY DIFFRACTIONc_mcangle_it2.6092
X-RAY DIFFRACTIONc_scbond_it1.7952
X-RAY DIFFRACTIONc_scangle_it2.8072.5
LS refinement shellResolution: 2.85→2.98 Å /
RfactorNum. reflection
Rfree0.342 30
Rwork0.358 -
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1protein_rep.paramprotein.top
X-RAY DIFFRACTION2dna-rna_rep.paramdna-rna.top
X-RAY DIFFRACTION3water_rep.paramwater.top
X-RAY DIFFRACTION4ion.paramion.top
X-RAY DIFFRACTION5carbohydrate.paramcarbohydrate.top

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