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- PDB-5s7g: XChem group deposition -- Crystal Structure of human ACVR1 in com... -

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Basic information

Entry
Database: PDB / ID: 5s7g
TitleXChem group deposition -- Crystal Structure of human ACVR1 in complex with XS035844b
ComponentsActivin receptor type-1
KeywordsTRANSFERASE / SGC - Diamond I04-1 fragment screening / PanDDA / XChemExplorer
Function / homology
Function and homology information


endocardial cushion cell fate commitment / mitral valve morphogenesis / atrial septum primum morphogenesis / endocardial cushion fusion / BMP receptor complex / BMP receptor activity / cardiac muscle cell fate commitment / activin receptor activity, type I / positive regulation of cardiac epithelial to mesenchymal transition / positive regulation of determination of dorsal identity ...endocardial cushion cell fate commitment / mitral valve morphogenesis / atrial septum primum morphogenesis / endocardial cushion fusion / BMP receptor complex / BMP receptor activity / cardiac muscle cell fate commitment / activin receptor activity, type I / positive regulation of cardiac epithelial to mesenchymal transition / positive regulation of determination of dorsal identity / acute inflammatory response / transforming growth factor beta receptor activity, type I / activin receptor complex / smooth muscle cell differentiation / endocardial cushion formation / receptor protein serine/threonine kinase / transmembrane receptor protein serine/threonine kinase activity / pharyngeal system development / activin binding / cellular response to BMP stimulus / activin receptor signaling pathway / negative regulation of activin receptor signaling pathway / transforming growth factor beta binding / embryonic heart tube morphogenesis / gastrulation with mouth forming second / dorsal/ventral pattern formation / determination of left/right symmetry / neural crest cell migration / atrioventricular valve morphogenesis / branching involved in blood vessel morphogenesis / negative regulation of G1/S transition of mitotic cell cycle / ventricular septum morphogenesis / SMAD binding / germ cell development / peptide hormone binding / positive regulation of SMAD protein signal transduction / mesoderm formation / regulation of ossification / positive regulation of osteoblast differentiation / BMP signaling pathway / positive regulation of bone mineralization / negative regulation of signal transduction / protein tyrosine kinase binding / transforming growth factor beta receptor signaling pathway / negative regulation of extrinsic apoptotic signaling pathway / cellular response to growth factor stimulus / positive regulation of peptidyl-tyrosine phosphorylation / apical part of cell / heart development / in utero embryonic development / protein kinase activity / positive regulation of cell migration / cadherin binding / phosphorylation / protein serine/threonine kinase activity / positive regulation of DNA-templated transcription / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / ATP binding / metal ion binding / plasma membrane
Similarity search - Function
GS domain / Transforming growth factor beta type I GS-motif / GS domain profile. / GS motif / Activin types I and II receptor domain / Activin types I and II receptor domain / Ser/Thr protein kinase, TGFB receptor / Snake toxin-like superfamily / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain ...GS domain / Transforming growth factor beta type I GS-motif / GS domain profile. / GS motif / Activin types I and II receptor domain / Activin types I and II receptor domain / Ser/Thr protein kinase, TGFB receptor / Snake toxin-like superfamily / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
Chem-LU8 / PROPANOIC ACID / Activin receptor type-1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / molecular replacement / Resolution: 1.78 Å
AuthorsWilliams, E.P. / Adamson, R.J. / Smil, D. / Krojer, T. / Burgess-Brown, N. / von Delft, F. / Bountra, C. / Bullock, A.N.
CitationJournal: To Be Published
Title: XChem group deposition
Authors: Williams, E.P. / Adamson, R.J. / Smil, D. / Krojer, T. / Burgess-Brown, N. / von Delft, F. / Bountra, C. / Bullock, A.N.
History
DepositionDec 11, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 23, 2021Provider: repository / Type: Initial release
Revision 1.1Mar 6, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Activin receptor type-1
B: Activin receptor type-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)72,50529
Polymers69,0752
Non-polymers3,43027
Water7,873437
1
A: Activin receptor type-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,84618
Polymers34,5381
Non-polymers2,30917
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Activin receptor type-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)35,65911
Polymers34,5381
Non-polymers1,12110
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)128.601, 84.591, 89.928
Angle α, β, γ (deg.)90.000, 131.460, 90.000
Int Tables number5
Space group name H-MC121

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Activin receptor type-1 / Activin receptor type I / ACTR-I / Activin receptor-like kinase 2 / ALK-2 / Serine/threonine- ...Activin receptor type I / ACTR-I / Activin receptor-like kinase 2 / ALK-2 / Serine/threonine-protein kinase receptor R1 / SKR1 / TGF-B superfamily receptor type I / TSR-I


Mass: 34537.633 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ACVR1, ACVRLK2 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm)
References: UniProt: Q04771, receptor protein serine/threonine kinase

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Non-polymers , 6 types, 464 molecules

#2: Chemical
ChemComp-LU8 / 4-methyl-3-[4-(1-methylpiperidin-4-yl)phenyl]-5-(3,4,5-trimethoxyphenyl)pyridine


Mass: 432.555 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C27H32N2O3
#3: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C2H6O2
#4: Chemical ChemComp-DMS / DIMETHYL SULFOXIDE / Dimethyl sulfoxide


Mass: 78.133 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#5: Chemical ChemComp-PPI / PROPANOIC ACID / Propionic acid


Mass: 74.079 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H6O2
#6: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: SO4
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 437 / 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: 2.65 Å3/Da / Density % sol: 53.64 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6
Details: 0.1M citrate pH 6.0, 1.4M ammonium sulfate, 0.2M sodium/potassium tartrate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9762 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jan 17, 2020
RadiationProtocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9762 Å / Relative weight: 1
ReflectionResolution: 1.78→42.31 Å / Num. obs: 68405 / % possible obs: 100 % / CC1/2: 1 / Rmerge(I) obs: 0.1 / Net I/σ(I): 9.3
Reflection shell

Diffraction-ID: 1 / Rejects: 0 / % possible all: 100

Resolution (Å)Rmerge(I) obsNum. unique allCC1/2Net I/σ(I) obs
1.78-1.813.31234510.330.3
4.83-42.310.0393544143.7

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
REFMAC5.8.0258refinement
Aimlessdata scaling
PDB_EXTRACT3.22data extraction
XDSdata reduction
REFMACphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 6SRH

6srh


Resolution: 1.78→42.33 Å / Cor.coef. Fo:Fc: 0.968 / Cor.coef. Fo:Fc free: 0.951 / SU B: 7.547 / SU ML: 0.188 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.127 / ESU R Free: 0.129 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2516 3281 4.8 %RANDOM
Rwork0.2037 ---
obs0.2059 65124 98.87 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 132.99 Å2 / Biso mean: 40.321 Å2 / Biso min: 20.02 Å2
Baniso -1Baniso -2Baniso -3
1--2.06 Å20 Å2-1.37 Å2
2---0.62 Å2-0 Å2
3---1.99 Å2
Refinement stepCycle: final / Resolution: 1.78→42.33 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4446 0 229 437 5112
Biso mean--55.91 51.98 -
Num. residues----565
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0134877
X-RAY DIFFRACTIONr_bond_other_d0.0010.0174501
X-RAY DIFFRACTIONr_angle_refined_deg1.5051.6816626
X-RAY DIFFRACTIONr_angle_other_deg1.2671.61610367
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.8595588
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.56121.485229
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.61215783
X-RAY DIFFRACTIONr_dihedral_angle_4_deg22.5051531
X-RAY DIFFRACTIONr_chiral_restr0.0710.2628
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.025348
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021057
X-RAY DIFFRACTIONr_mcbond_it3.0644.1452313
X-RAY DIFFRACTIONr_mcbond_other3.0644.1432312
X-RAY DIFFRACTIONr_mcangle_it4.6386.1872902
LS refinement shellResolution: 1.78→1.826 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.5 242 -
Rwork0.502 4205 -
all-4447 -
obs--87.11 %

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