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- PDB-1rap: THE STRUCTURE AND FUNCTION OF OMEGA LOOP A REPLACEMENTS IN CYTOCH... -

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Basic information

Entry
Database: PDB / ID: 1rap
TitleTHE STRUCTURE AND FUNCTION OF OMEGA LOOP A REPLACEMENTS IN CYTOCHROME C
ComponentsREP A2 ISO-1-CYTOCHROME C
KeywordsELECTRON TRANSPORT
Function / homology
Function and homology information


Release of apoptotic factors from the mitochondria / Pyroptosis / Detoxification of Reactive Oxygen Species / Respiratory electron transport / cardiolipin binding / mitochondrial electron transport, cytochrome c to oxygen / mitochondrial electron transport, ubiquinol to cytochrome c / mitochondrial intermembrane space / electron transfer activity / heme binding ...Release of apoptotic factors from the mitochondria / Pyroptosis / Detoxification of Reactive Oxygen Species / Respiratory electron transport / cardiolipin binding / mitochondrial electron transport, cytochrome c to oxygen / mitochondrial electron transport, ubiquinol to cytochrome c / 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 / Resolution: 2.25 Å
AuthorsMurphy, M.E.P. / Brayer, G.D.
Citation
Journal: Protein Sci. / Year: 1993
Title: The structure and function of omega loop A replacements in cytochrome c.
Authors: Murphy, M.E. / Fetrow, J.S. / Burton, R.E. / Brayer, G.D.
#1: Journal: J.Mol.Biol. / Year: 1990
Title: High-Resolution Refinement of Yeast Iso-1-Cytochrome C and Comparisons with Other Eukaryotic Cytochromes C
Authors: Louie, G.V. / Brayer, G.D.
#2: Journal: Proteins / Year: 1989
Title: Deletions and Replacements of Omega Loops in Yeast Iso-1-Cytochrome C
Authors: Fetrow, J.S. / Cardillo, T.S. / Sherman, F.
#3: Journal: J.Mol.Biol. / Year: 1988
Title: Yeast Iso-1-Cytochrome C: A 2.8 Angstroms Resolution Three-Dimensional Structure Determination
Authors: Louie, G.V. / Hutcheon, W.L.B. / Brayer, G.D.
History
DepositionAug 25, 1992Processing site: BNL
Revision 1.0Oct 31, 1993Provider: repository / Type: Initial release
Revision 1.1Mar 21, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4Mar 26, 2025Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / 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_entry_details.has_protein_modification / _struct_conn.pdbx_leaving_atom_flag / _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: REP A2 ISO-1-CYTOCHROME C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)12,8113
Polymers12,0991
Non-polymers7132
Water91951
1
A: REP A2 ISO-1-CYTOCHROME C
hetero molecules

A: REP A2 ISO-1-CYTOCHROME C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,6236
Polymers24,1982
Non-polymers1,4254
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation7_465y-1,x+1,-z1
Unit cell
Length a, b, c (Å)36.380, 36.380, 137.630
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212

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Components

#1: Protein REP A2 ISO-1-CYTOCHROME C


Mass: 12098.800 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
References: UniProt: P00044
#2: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4
#3: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 51 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY
Sequence detailsAMINO ACID NUMBERING FOLLOWS THAT OF AN ALIGNMENT TO VERTEBRATE CYTOCHROMES C. THE N-TERMINAL ...AMINO ACID NUMBERING FOLLOWS THAT OF AN ALIGNMENT TO VERTEBRATE CYTOCHROMES C. THE N-TERMINAL RESIDUE IS THR -5; THE C-TERMINAL RESIDUE IS GLU 103 (SEE MURPHY ET AL., 1993).

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 1.89 Å3/Da / Density % sol: 34.85 %
Crystal grow
*PLUS
pH: 5.5 / Method: macro-seeding hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
195 %1reservoir(NH4)2SO4
20.07 M1reservoirNa2S2O4
30.1 Msodium phosphate1reservoir

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1
Reflection
*PLUS
Highest resolution: 2.25 Å / Num. all: 25731 / Num. obs: 4498 / % possible obs: 86 % / Rmerge(I) obs: 0.073

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Processing

SoftwareName: PROLSQ / Classification: refinement
RefinementHighest resolution: 2.25 Å / σ(F): 2 /
RfactorNum. reflection
obs0.183 4197
Refinement stepCycle: LAST / Highest resolution: 2.25 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms846 0 51 51 948
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONp_bond_d0.018
X-RAY DIFFRACTIONp_angle_d
X-RAY DIFFRACTIONp_angle_deg
X-RAY DIFFRACTIONp_planar_d
X-RAY DIFFRACTIONp_hb_or_metal_coord
X-RAY DIFFRACTIONp_mcbond_it
X-RAY DIFFRACTIONp_mcangle_it
X-RAY DIFFRACTIONp_scbond_it
X-RAY DIFFRACTIONp_scangle_it
X-RAY DIFFRACTIONp_plane_restr
X-RAY DIFFRACTIONp_chiral_restr
X-RAY DIFFRACTIONp_singtor_nbd
X-RAY DIFFRACTIONp_multtor_nbd
X-RAY DIFFRACTIONp_xhyhbond_nbd
X-RAY DIFFRACTIONp_xyhbond_nbd
X-RAY DIFFRACTIONp_planar_tor
X-RAY DIFFRACTIONp_staggered_tor
X-RAY DIFFRACTIONp_orthonormal_tor
X-RAY DIFFRACTIONp_transverse_tor
X-RAY DIFFRACTIONp_special_tor
Software
*PLUS
Name: PROLSQ / Classification: refinement
Refinement
*PLUS
Highest resolution: 2.25 Å / Num. reflection obs: 4197 / σ(F): 2 / Rfactor obs: 0.183
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal targetDev ideal
X-RAY DIFFRACTIONp_bond_d0.02
X-RAY DIFFRACTIONp_angle_d0.030.042
X-RAY DIFFRACTIONp_planar_d0.050.053
X-RAY DIFFRACTIONp_plane_restr0.020.013
X-RAY DIFFRACTIONp_chiral_restr0.160.21

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