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- PDB-4qao: Lysine-ligated cytochrome c with F82H -

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Basic information

Entry
Database: PDB / ID: 4qao
TitleLysine-ligated cytochrome c with F82H
ComponentsCytochrome c iso-1
KeywordsELECTRON TRANSPORT
Function / homology
Function and homology information


Release of apoptotic factors from the mitochondria / Pyroptosis / Detoxification of Reactive Oxygen Species / Respiratory electron transport / mitochondrial electron transport, cytochrome c to oxygen / mitochondrial electron transport, ubiquinol to cytochrome c / respirasome / mitochondrial intermembrane space / electron transfer activity / heme binding ...Release of apoptotic factors from the mitochondria / Pyroptosis / Detoxification of Reactive Oxygen Species / Respiratory electron transport / mitochondrial electron transport, cytochrome c to oxygen / mitochondrial electron transport, ubiquinol to cytochrome c / respirasome / mitochondrial intermembrane space / electron transfer activity / heme binding / mitochondrion / metal ion binding
Similarity search - Function
Cytochrome c, class IA/ IB / Cytochrome c / Cytochrome c-like domain / Cytochrome Bc1 Complex; Chain D, domain 2 / Cytochrome c family profile. / Cytochrome c-like domain / Cytochrome c-like domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
PROTOPORPHYRIN IX CONTAINING FE / Cytochrome c isoform 1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.103 Å
AuthorsAmacher, J.F. / Zhu, M.Q. / Zhong, F. / Pletneva, E.K. / Madden, D.R.
CitationJournal: Thesis / Year: 2014
Title: Understanding PDZ Affinity and Selectivity: All Residues Considered
Authors: Amacher, J.F.
History
DepositionMay 5, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 5, 2015Provider: repository / Type: Initial release
Revision 1.1Nov 22, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.2Jul 17, 2019Group: Data collection / Refinement description / Category: software
Item: _software.classification / _software.name / _software.version
Revision 1.3Sep 20, 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 / pdbx_struct_conn_angle / struct_conn / 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 / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_label_asym_id / _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: Cytochrome c iso-1
B: Cytochrome c iso-1
C: Cytochrome c iso-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,9206
Polymers35,0713
Non-polymers1,8493
Water1,69394
1
A: Cytochrome c iso-1
hetero molecules

A: Cytochrome c iso-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,6144
Polymers23,3812
Non-polymers1,2332
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_565-x,-y+1,z1
Buried area3940 Å2
ΔGint-64 kcal/mol
Surface area10660 Å2
MethodPISA
2
B: Cytochrome c iso-1
hetero molecules

B: Cytochrome c iso-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,6144
Polymers23,3812
Non-polymers1,2332
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation16_555-y+1/2,-x+1/2,-z+1/21
Buried area3900 Å2
ΔGint-63 kcal/mol
Surface area10700 Å2
MethodPISA
3
C: Cytochrome c iso-1
hetero molecules

C: Cytochrome c iso-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,6144
Polymers23,3812
Non-polymers1,2332
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation7_556y,x,-z+11
Buried area3950 Å2
ΔGint-65 kcal/mol
Surface area10930 Å2
MethodPISA
Unit cell
Length a, b, c (Å)105.960, 105.960, 149.950
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number97
Space group name H-MI422

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Components

#1: Protein Cytochrome c iso-1


Mass: 11690.332 Da / Num. of mol.: 3 / Fragment: UNP residues 8-109 / Mutation: T78C, K79G, F82H
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: CYC1, YJR048W, J1653 / Production host: Escherichia coli (E. coli) / References: UniProt: P00044
#2: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME / Heme B


Mass: 616.487 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 94 / 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: 3.11 Å3/Da / Density % sol: 60.42 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8
Details: 28% w/v PEG, 0.3 M ammonium phosphate, 0.1 M Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X6A / Wavelength: 1.0781 Å
DetectorType: ADSC QUANTUM 270 / Detector: CCD / Date: Nov 11, 2013
RadiationMonochromator: channel cut Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0781 Å / Relative weight: 1
Reflection twin
Crystal-IDIDOperatorDomain-IDFraction
11H, K, L10.328
11-1/2H-1/2K+1/2L, -1/2H-1/2K-1/2L, H-K20.329
11-1/2H+1/2K+1/2L, 1/2H-1/2K+1/2L, H+K30.343
ReflectionResolution: 2.103→19.52 Å / Num. all: 25279 / Num. obs: 25155 / % possible obs: 99.5 % / Observed criterion σ(F): 1.36 / Observed criterion σ(I): 8.48 / Redundancy: 29.1 % / Rsym value: 0.095 / Net I/σ(I): 39.39
Reflection shell
Resolution (Å)Redundancy (%)Mean I/σ(I) obsRsym valueDiffraction-ID% possible all
2.103-2.2229.28.480.549198.2
2.23-2.3729.311.560.4121100
2.38-2.5629.515.370.2981100
2.57-2.829.423.770.181100
2.81-3.1229.335.940.1121100
3.13-3.5929.360.130.0621100

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Processing

Software
NameVersionClassification
REFMAC5.8.0107refinement
PHENIXmodel building
PHENIX(phenix.refine: 1.7_650)refinement
XDSdata reduction
XSCALEdata scaling
PHENIXphasing
Blu-Icedata collection
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4Q5P

4q5p


Resolution: 2.103→19.52 Å / Cor.coef. Fo:Fc: 0.942 / Cor.coef. Fo:Fc free: 0.915 / SU B: 3.939 / SU ML: 0.113 / Cross valid method: THROUGHOUT / ESU R: 0.037 / ESU R Free: 0.034 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.22318 1311 5.2 %RANDOM
Rwork0.1827 ---
obs0.18484 23843 99.74 %-
all-25155 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 30.737 Å2
Baniso -1Baniso -2Baniso -3
1--2.19 Å2-0 Å2-0 Å2
2---2.19 Å2-0 Å2
3---4.38 Å2
Refinement stepCycle: LAST / Resolution: 2.103→19.52 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2460 0 129 94 2683
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0210.0192664
X-RAY DIFFRACTIONr_bond_other_d0.0070.022496
X-RAY DIFFRACTIONr_angle_refined_deg1.9792.0263615
X-RAY DIFFRACTIONr_angle_other_deg1.24235760
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.475315
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.80124.444108
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.86615459
X-RAY DIFFRACTIONr_dihedral_angle_4_deg11.118159
X-RAY DIFFRACTIONr_chiral_restr0.1360.2348
X-RAY DIFFRACTIONr_gen_planes_refined0.0130.023051
X-RAY DIFFRACTIONr_gen_planes_other0.0180.02636
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_it3.5452.9341269
X-RAY DIFFRACTIONr_mcbond_other3.5282.9321268
X-RAY DIFFRACTIONr_mcangle_it4.734.3891581
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it3.453.081391
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.103→2.157 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.2 66 -
Rwork0.164 1788 -
obs--99.68 %

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