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- PDB-6fug: Complement factor D in complex with the inhibitor 3-((3-((3-(amin... -

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Basic information

Entry
Database: PDB / ID: 6fug
TitleComplement factor D in complex with the inhibitor 3-((3-((3-(aminomethyl)phenyl)amino)-1H-pyrazolo[3,4-d]pyrimidin-4-yl)amino)phenol
ComponentsComplement factor DFactor D
KeywordsHYDROLASE / SERINE PROTEASE / inhibitor / complex
Function / homology
Function and homology information


complement factor D / Alternative complement activation / complement activation, alternative pathway / complement activation / serine-type peptidase activity / platelet alpha granule lumen / response to bacterium / Platelet degranulation / secretory granule lumen / ficolin-1-rich granule lumen ...complement factor D / Alternative complement activation / complement activation, alternative pathway / complement activation / serine-type peptidase activity / platelet alpha granule lumen / response to bacterium / Platelet degranulation / secretory granule lumen / ficolin-1-rich granule lumen / serine-type endopeptidase activity / Neutrophil degranulation / proteolysis / extracellular exosome / extracellular region
Similarity search - Function
Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin domain profile. / Serine proteases, trypsin family, serine active site. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Trypsin-like serine proteases ...Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin domain profile. / Serine proteases, trypsin family, serine active site. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Trypsin-like serine proteases / Thrombin, subunit H / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Chem-E85 / Complement factor D
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.21 Å
AuthorsMac Sweeney, A. / Ostermann, N. / Vulpetti, A. / Maibaum, J. / Erbel, P. / Lorthiois, E. / Yoon, T. / Randl, S. / Ruedisser, S.
CitationJournal: ACS Med Chem Lett / Year: 2018
Title: Discovery and Design of First Benzylamine-Based Ligands Binding to an Unlocked Conformation of the Complement Factor D.
Authors: Vulpetti, A. / Ostermann, N. / Randl, S. / Yoon, T. / Mac Sweeney, A. / Cumin, F. / Lorthiois, E. / Rudisser, S. / Erbel, P. / Maibaum, J.
History
DepositionFeb 27, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 6, 2018Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Complement factor D
B: Complement factor D
C: Complement factor D
D: Complement factor D
E: Complement factor D
F: Complement factor D
hetero molecules


Theoretical massNumber of molelcules
Total (without water)150,51912
Polymers148,4356
Non-polymers2,0846
Water5,134285
1
A: Complement factor D
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,0862
Polymers24,7391
Non-polymers3471
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Complement factor D
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,0862
Polymers24,7391
Non-polymers3471
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Complement factor D
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,0862
Polymers24,7391
Non-polymers3471
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Complement factor D
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,0862
Polymers24,7391
Non-polymers3471
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: Complement factor D
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,0862
Polymers24,7391
Non-polymers3471
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
F: Complement factor D
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,0862
Polymers24,7391
Non-polymers3471
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)66.523, 68.482, 73.380
Angle α, β, γ (deg.)95.21, 116.70, 102.43
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14A
24E
15A
25F
16B
26C
17B
27D
18B
28E
19B
29F
110C
210D
111C
211E
112C
212F
113D
213E
114D
214F
115E
215F

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1010A16 - 243
2010B16 - 243
1020A16 - 245
2020C16 - 245
1030A16 - 245
2030D16 - 245
1040A16 - 245
2040E16 - 245
1050A16 - 245
2050F16 - 245
1060B16 - 243
2060C16 - 243
1070B16 - 242
2070D16 - 242
1080B16 - 243
2080E16 - 243
1090B16 - 243
2090F16 - 243
10100C16 - 245
20100D16 - 245
10110C16 - 245
20110E16 - 245
10120C16 - 245
20120F16 - 245
10130D16 - 245
20130E16 - 245
10140D16 - 245
20140F16 - 245
10150E16 - 245
20150F16 - 245

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15

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Components

#1: Protein
Complement factor D / Factor D / Adipsin / C3 convertase activator / Properdin factor D


Mass: 24739.121 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CFD, DF, PFD / Production host: Escherichia coli (E. coli) / References: UniProt: P00746, complement factor D
#2: Chemical
ChemComp-E85 / 3-[[3-[[3-(aminomethyl)phenyl]amino]-1~{H}-pyrazolo[3,4-d]pyrimidin-4-yl]amino]phenol


Mass: 347.374 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C18H17N7O / Feature type: SUBJECT OF INVESTIGATION
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 285 / 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

Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: 25% PEG3350, 100 mM TRIS pH 8.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Jun 6, 2010
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.21→50.8 Å / Num. obs: 52329 / % possible obs: 94.3 % / Redundancy: 2 % / Net I/σ(I): 13.3
Reflection shellResolution: 2.21→2.28 Å / Rmerge(I) obs: 0.237 / Mean I/σ(I) obs: 3.33

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Processing

Software
NameVersionClassification
REFMAC5.8.0189refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.21→46.11 Å / Cor.coef. Fo:Fc: 0.937 / Cor.coef. Fo:Fc free: 0.919 / SU B: 8.687 / SU ML: 0.214 / Cross valid method: THROUGHOUT / ESU R: 0.531 / ESU R Free: 0.268 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.25905 2617 5 %RANDOM
Rwork0.22127 ---
obs0.22316 49708 94.64 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 42.556 Å2
Baniso -1Baniso -2Baniso -3
1-0.05 Å20.01 Å2-0.07 Å2
2--0.31 Å2-0.27 Å2
3----0.07 Å2
Refinement stepCycle: 1 / Resolution: 2.21→46.11 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9568 0 156 285 10009
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.01910077
X-RAY DIFFRACTIONr_bond_other_d0.0030.029400
X-RAY DIFFRACTIONr_angle_refined_deg1.6711.98713756
X-RAY DIFFRACTIONr_angle_other_deg1.017321714
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.99751301
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.83123.197391
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.969151557
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.3641585
X-RAY DIFFRACTIONr_chiral_restr0.0850.21559
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.02111276
X-RAY DIFFRACTIONr_gen_planes_other0.010.021979
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_it3.4584.0945188
X-RAY DIFFRACTIONr_mcbond_other3.4584.0935187
X-RAY DIFFRACTIONr_mcangle_it5.2366.1126463
X-RAY DIFFRACTIONr_mcangle_other5.2356.1136464
X-RAY DIFFRACTIONr_scbond_it3.7454.5614889
X-RAY DIFFRACTIONr_scbond_other3.7444.564890
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other5.7956.6577284
X-RAY DIFFRACTIONr_long_range_B_refined8.35648.38910551
X-RAY DIFFRACTIONr_long_range_B_other8.34848.37210523
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A127760.05
12B127760.05
21A130120.04
22C130120.04
31A129860.04
32D129860.04
41A128200.05
42E128200.05
51A128320.05
52F128320.05
61B129780.04
62C129780.04
71B130120.05
72D130120.05
81B129740.04
82E129740.04
91B129420.05
92F129420.05
101C129520.05
102D129520.05
111C127520.05
112E127520.05
121C127680.05
122F127680.05
131D129200.05
132E129200.05
141D129100.05
142F129100.05
151E130680.04
152F130680.04
LS refinement shellResolution: 2.21→2.267 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.347 193 -
Rwork0.281 3660 -
obs--94.3 %

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