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- PDB-3rcf: Human cyclophilin D complexed with N-[(4-aminophenyl)sulfonyl]ben... -

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Basic information

Entry
Database: PDB / ID: 3rcf
TitleHuman cyclophilin D complexed with N-[(4-aminophenyl)sulfonyl]benzamide
ComponentsPeptidyl-prolyl cis-trans isomerase F, mitochondrial
KeywordsISOMERASE/ISOMERASE INHIBITOR / beta barrel / prolyl cis/trans isomerase / mitochondria / inhibitor / ISOMERASE-ISOMERASE INHIBITOR complex
Function / homology
Function and homology information


: / : / mitochondrial outer membrane permeabilization involved in programmed cell death / regulation of mitochondrial membrane permeability involved in programmed necrotic cell death / skeletal muscle fiber differentiation / mitochondrial permeability transition pore complex / cellular response to arsenic-containing substance / negative regulation of ATP-dependent activity / mitochondrial depolarization / negative regulation of oxidative phosphorylation ...: / : / mitochondrial outer membrane permeabilization involved in programmed cell death / regulation of mitochondrial membrane permeability involved in programmed necrotic cell death / skeletal muscle fiber differentiation / mitochondrial permeability transition pore complex / cellular response to arsenic-containing substance / negative regulation of ATP-dependent activity / mitochondrial depolarization / negative regulation of oxidative phosphorylation / regulation of mitochondrial membrane permeability / cyclosporin A binding / negative regulation of release of cytochrome c from mitochondria / negative regulation of intrinsic apoptotic signaling pathway / necroptotic process / apoptotic mitochondrial changes / cellular response to calcium ion / response to ischemia / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / cellular response to hydrogen peroxide / protein folding / mitochondrial matrix / negative regulation of apoptotic process / mitochondrion / membrane / cytoplasm
Similarity search - Function
Cyclophilin-like / Cyclophilin / Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site / Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. / Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain profile. / Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain / Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD / Cyclophilin-like domain superfamily / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
N-[(4-aminophenyl)sulfonyl]benzamide / Peptidyl-prolyl cis-trans isomerase F, mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.15 Å
AuthorsColliandre, L. / Ahmed-Belkacem, H. / Bessin, Y. / Pawlotsky, J.M. / Guichou, J.F.
CitationJournal: Nat Commun / Year: 2016
Title: Fragment-based discovery of a new family of non-peptidic small-molecule cyclophilin inhibitors with potent antiviral activities.
Authors: Ahmed-Belkacem, A. / Colliandre, L. / Ahnou, N. / Nevers, Q. / Gelin, M. / Bessin, Y. / Brillet, R. / Cala, O. / Douguet, D. / Bourguet, W. / Krimm, I. / Pawlotsky, J.M. / Guichou, J.F.
History
DepositionMar 31, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 21, 2012Provider: repository / Type: Initial release
Revision 1.1Dec 5, 2012Group: Structure summary
Revision 1.2Oct 19, 2016Group: Database references
Revision 1.3Sep 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / 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 / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Peptidyl-prolyl cis-trans isomerase F, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,4233
Polymers17,8701
Non-polymers5532
Water7,530418
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)57.518, 57.518, 87.564
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212
Components on special symmetry positions
IDModelComponents
11A-420-

HOH

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Components

#1: Protein Peptidyl-prolyl cis-trans isomerase F, mitochondrial / PPIase F / Cyclophilin F / Rotamase F


Mass: 17870.400 Da / Num. of mol.: 1 / Fragment: UNP residues 43-207 / Mutation: K175I
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PPIF, CYP3 / Production host: Escherichia coli (E. coli) / References: UniProt: P30405, peptidylprolyl isomerase
#2: Chemical ChemComp-BS4 / N-[(4-aminophenyl)sulfonyl]benzamide


Mass: 276.311 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C13H12N2O3S
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 418 / 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: 2.03 Å3/Da / Density % sol: 39.3 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.3
Details: 30% PEG4000, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Feb 15, 2007
RadiationMonochromator: yale mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.933 Å / Relative weight: 1
ReflectionResolution: 1.15→27.3 Å / Num. all: 50252 / Num. obs: 49247 / % possible obs: 98.2 % / Observed criterion σ(F): 19.9 / Observed criterion σ(I): 19.9 / Redundancy: 7.3 % / Rsym value: 0.065
Reflection shellResolution: 1.15→1.18 Å / Redundancy: 6.3 % / Rsym value: 0.263 / % possible all: 90.9

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Processing

Software
NameVersionClassification
DNAdata collection
X-PLORmodel building
REFMAC5.2.0019refinement
MOSFLMdata reduction
SCALAdata scaling
X-PLORphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2BIT

2bit


Resolution: 1.15→26.03 Å / Cor.coef. Fo:Fc: 0.979 / Cor.coef. Fo:Fc free: 0.969 / SU B: 0.836 / SU ML: 0.018 / Cross valid method: THROUGHOUT / ESU R: 0.035 / ESU R Free: 0.034 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.15 2583 5 %RANDOM
Rwork0.12516 ---
all0.126 50252 --
obs0.1264 49247 98.06 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 5.305 Å2
Baniso -1Baniso -2Baniso -3
1-0.01 Å20 Å20 Å2
2--0.01 Å20 Å2
3----0.03 Å2
Refinement stepCycle: LAST / Resolution: 1.15→26.03 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1237 0 38 418 1693
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.0211409
X-RAY DIFFRACTIONr_bond_other_d0.0040.02982
X-RAY DIFFRACTIONr_angle_refined_deg1.1641.9791914
X-RAY DIFFRACTIONr_angle_other_deg0.8263.0032392
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.9585181
X-RAY DIFFRACTIONr_dihedral_angle_2_deg32.27523.89859
X-RAY DIFFRACTIONr_dihedral_angle_3_deg10.33415252
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.075157
X-RAY DIFFRACTIONr_chiral_restr0.0750.2207
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.021575
X-RAY DIFFRACTIONr_gen_planes_other0.0040.02286
X-RAY DIFFRACTIONr_nbd_refined0.2230.2257
X-RAY DIFFRACTIONr_nbd_other0.1890.21065
X-RAY DIFFRACTIONr_nbtor_refined0.1750.2701
X-RAY DIFFRACTIONr_nbtor_other0.0850.2673
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1270.2280
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.0740.23
X-RAY DIFFRACTIONr_symmetry_vdw_other0.1890.240
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.0790.293
X-RAY DIFFRACTIONr_mcbond_it0.5881.5885
X-RAY DIFFRACTIONr_mcbond_other0.2021.5353
X-RAY DIFFRACTIONr_mcangle_it0.85621379
X-RAY DIFFRACTIONr_scbond_it1.0333628
X-RAY DIFFRACTIONr_scangle_it1.2954.5528
X-RAY DIFFRACTIONr_rigid_bond_restr0.45632674
X-RAY DIFFRACTIONr_sphericity_free1.9793483
X-RAY DIFFRACTIONr_sphericity_bonded1.09732351
LS refinement shellResolution: 1.15→1.18 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.19 178 -
Rwork0.158 3095 -
obs--85.26 %

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