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- PDB-5sbr: CD44 PanDDA analysis group deposition -- The hyaluronan-binding d... -

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Basic information

Entry
Database: PDB / ID: 5sbr
TitleCD44 PanDDA analysis group deposition -- The hyaluronan-binding domain of CD44 in complex with Z1259341012
ComponentsCD44 antigen
KeywordsPROTEIN BINDING / SGC - Diamond I04-1 fragment screening / PanDDA / XChemExplorer / antigen
Function / homology
Function and homology information


Hyaluronan uptake and degradation / positive regulation of monocyte aggregation / hyaluronic acid binding / macrophage fusion / macrophage migration inhibitory factor receptor complex / Degradation of the extracellular matrix / negative regulation of regulatory T cell differentiation / regulation of lamellipodium morphogenesis / Integrin cell surface interactions / Cell surface interactions at the vascular wall ...Hyaluronan uptake and degradation / positive regulation of monocyte aggregation / hyaluronic acid binding / macrophage fusion / macrophage migration inhibitory factor receptor complex / Degradation of the extracellular matrix / negative regulation of regulatory T cell differentiation / regulation of lamellipodium morphogenesis / Integrin cell surface interactions / Cell surface interactions at the vascular wall / hyaluronan catabolic process / wound healing involved in inflammatory response / monocyte aggregation / positive regulation of adaptive immune response / branching involved in prostate gland morphogenesis / type II transforming growth factor beta receptor binding / negative regulation of CD4-positive, alpha-beta T cell proliferation / negative regulation of mature B cell apoptotic process / positive regulation of neutrophil apoptotic process / channel regulator activity / cellular response to fibroblast growth factor stimulus / cargo receptor activity / positive regulation of heterotypic cell-cell adhesion / wound healing, spreading of cells / branching involved in ureteric bud morphogenesis / epidermal growth factor receptor binding / negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / negative regulation of DNA damage response, signal transduction by p53 class mediator / microvillus / lamellipodium membrane / Neutrophil degranulation / T cell activation / receptor-mediated endocytosis / cell projection / regulation of cell growth / phosphoprotein binding / Wnt signaling pathway / negative regulation of inflammatory response / cytokine-mediated signaling pathway / neuron projection development / cell migration / positive regulation of peptidyl-tyrosine phosphorylation / transmembrane signaling receptor activity / positive regulation of peptidyl-serine phosphorylation / basolateral plasma membrane / positive regulation of ERK1 and ERK2 cascade / cell adhesion / inflammatory response / membrane raft / apical plasma membrane / external side of plasma membrane / positive regulation of gene expression / negative regulation of apoptotic process / protein kinase binding / Golgi apparatus / cell surface / protein-containing complex / extracellular region / plasma membrane / cytosol
Similarity search - Function
CD44 antigen / CD44 antigen-like / Link domain / Extracellular link domain / Link domain signature. / Link domain profile. / Link (Hyaluronan-binding) / C-type lectin-like/link domain superfamily / C-type lectin fold
Similarity search - Domain/homology
(1R)-1-[4-(morpholin-4-yl)phenyl]ethan-1-amine / CD44 antigen
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / molecular replacement / Resolution: 1.286 Å
AuthorsBradshaw, W.J. / Katis, V.L. / Bezerra, G.A. / Koekemoer, L. / von Delft, F. / Bountra, C. / Brennan, P.E. / Gileadi, O.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute on Aging (NIH/NIA)1RF1AG057443 United States
CitationJournal: To Be Published
Title: CD44 PanDDA analysis group deposition
Authors: Bradshaw, W.J. / Katis, V.L. / Bezerra, G.A. / Koekemoer, L. / von Delft, F. / Bountra, C. / Brennan, P.E. / Gileadi, O.
History
DepositionSep 14, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 22, 2021Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: CD44 antigen
hetero molecules


Theoretical massNumber of molelcules
Total (without water)17,4746
Polymers16,9711
Non-polymers5035
Water4,252236
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)30.656, 81.015, 31.854
Angle α, β, γ (deg.)90.000, 117.790, 90.000
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein CD44 antigen / Extracellular matrix receptor III / ECMR-III / GP90 lymphocyte homing/adhesion receptor / HUTCH-I / ...Extracellular matrix receptor III / ECMR-III / GP90 lymphocyte homing/adhesion receptor / HUTCH-I / Hermes antigen / Hyaluronate receptor / Lymphocyte antigen 24 / Ly-24 / Phagocytic glycoprotein 1 / PGP-1 / Phagocytic glycoprotein I / PGP-I


Mass: 16970.891 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Cd44, Ly-24 / Production host: Escherichia coli (E. coli) / References: UniProt: P15379
#2: Chemical ChemComp-8B2 / (1R)-1-[4-(morpholin-4-yl)phenyl]ethan-1-amine


Mass: 206.284 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C12H18N2O / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-DMS / DIMETHYL SULFOXIDE / Dimethyl sulfoxide


Mass: 78.133 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#4: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6O2
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 236 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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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: 2.06 Å3/Da / Density % sol: 40.35 % / Mosaicity: 0.22 °
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 200mM ammonium sulphate, 100mM MES, 24% PEG 5,000 MME

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.91199 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 6, 2021
RadiationProtocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelengthWavelength: 0.91199 Å / Relative weight: 1
ReflectionResolution: 1.29→40.51 Å / Num. obs: 33209 / % possible obs: 95.4 % / Redundancy: 3.8 % / Biso Wilson estimate: 9.28 Å2 / CC1/2: 0.904 / Rmerge(I) obs: 0.288 / Rpim(I) all: 0.191 / Rrim(I) all: 0.348 / Net I/σ(I): 5.6 / Num. measured all: 124633 / Scaling rejects: 4642
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique allCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
1.29-1.363.91.1061841447360.5150.6651.2951.993.5
4.07-40.513.70.056404911070.9930.0350.06613.698.1

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
BUSTER2.10.4 (20-APR-2021)refinement
Aimless0.7.4data scaling
PDB_EXTRACT3.23data extraction
XDSdata reduction
REFMACphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 2JCP

2jcp


Resolution: 1.286→40.51 Å / Cor.coef. Fo:Fc: 0.931 / Cor.coef. Fo:Fc free: 0.939 / SU R Cruickshank DPI: 0.061 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.067 / SU Rfree Blow DPI: 0.067 / SU Rfree Cruickshank DPI: 0.063
RfactorNum. reflection% reflectionSelection details
Rfree0.207 1483 5.01 %RANDOM
Rwork0.1788 ---
obs0.1802 29620 84.9 %-
Displacement parametersBiso max: 63.59 Å2 / Biso mean: 13.64 Å2 / Biso min: 6.49 Å2
Baniso -1Baniso -2Baniso -3
1-0.9843 Å20 Å2-0.3575 Å2
2---5.0352 Å20 Å2
3---4.0509 Å2
Refine analyzeLuzzati coordinate error obs: 0.17 Å
Refinement stepCycle: final / Resolution: 1.286→40.51 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1171 0 31 240 1442
Biso mean--14.14 26.11 -
Num. residues----150
Refine LS restraints
Refine-IDTypeNumberRestraint functionWeightDev ideal
X-RAY DIFFRACTIONt_dihedral_angle_d473SINUSOIDAL2
X-RAY DIFFRACTIONt_trig_c_planes
X-RAY DIFFRACTIONt_gen_planes238HARMONIC5
X-RAY DIFFRACTIONt_it1285HARMONIC10
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_chiral_improper_torsion179SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact1724SEMIHARMONIC4
X-RAY DIFFRACTIONt_bond_d1313HARMONIC20.01
X-RAY DIFFRACTIONt_angle_deg1797HARMONIC21.16
X-RAY DIFFRACTIONt_omega_torsion5.47
X-RAY DIFFRACTIONt_other_torsion15.08
LS refinement shellResolution: 1.29→1.3 Å / Total num. of bins used: 51
RfactorNum. reflection% reflection
Rfree0.2465 38 6.41 %
Rwork0.2346 555 -
all-593 -
obs--72.44 %

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