2bcc

STIGMATELLIN-BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN

Method: X-RAY DIFFRACTION

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1. Protein Identity and Related Structures Protein Identity & Related Structures

UBIQUINOL CYTOCHROME C OXIDOREDUCTASE

OrganismNot specified

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain C； UniProt 1–380	Not recorded	UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 1 UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 1 UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 1 UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 1 UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 1 UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 1 UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 1 UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 1 UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 3 U10 UBIQUINONE-10 × 1 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 2 SIG STIGMATELLIN × 1 BOG octyl beta-D-glucopyranoside × 1 FES FE2/S2 (INORGANIC) CLUSTER × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.7；20MM KMES PH6.7, 75MM NACL, 10% GLYCEROL, AND 6% PEG4000, INHIBITOR WAS ADDED FROM ETHANOLIC SOLUTION	Resolution 3.50 Å R-free 0.317

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 2BCC	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BCC CYTOCHROME BC1 COMPLEX FROM CHICKEN Deposited 1998-03-23	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-MERIC	Chain C 1–380（380 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 6 U10 UBIQUINONE-10 × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 4 BOG octyl beta-D-glucopyranoside × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.7；20MM KMES PH6.7, 75MM NACL, 10% GLYCEROL, AND 6% PEG4000	Resolution 3.16 Å R-free 0.310
3BCC STIGMATELLIN AND ANTIMYCIN BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN Deposited 1998-03-23	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-MERIC	Chain C 1–380（380 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 6 SIG STIGMATELLIN × 2 AMY ANTIMYCIN × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.7；20MM KMES PH6.7, 75MM NACL, 10% GLYCEROL, AND 6% PEG4000, INHIBITOR WAS ADDED FROM ETHANOLIC SOLUTION	Resolution 3.70 Å R-free 0.321
3CWB Chicken Cytochrome BC1 Complex inhibited by an iodinated analogue of the polyketide Crocacin-D Deposited 2008-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain C 1–380（380 aa） Chain P 1–380（380 aa）	Not recorded	PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 BOG octyl beta-D-glucopyranoside × 6 AZI AZIDE ION × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 ICX methyl N-[(5Z)-6-({[4-(4-iodobenzyl)phenyl]carbonyl}amino)hex-5-enoyl]glycinate × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 FES FE2/S2 (INORGANIC) CLUSTER × 2 UNL UNKNOWN LIGAND × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.7；277 K；20MM KMES, 75MM NACL, 10% GLYCEROL, 6% PEG4000. Crystal soaked with the inhibitor and RbBr salt, pH 6.7, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 3.51 Å R-free 0.319
3H1H Cytochrome bc1 complex from chicken Deposited 2009-04-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain C 1–380（380 aa） Chain P 1–380（380 aa）	Not recorded	UNL UNKNOWN LIGAND × 9 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 CDL CARDIOLIPIN × 4 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 GOL GLYCEROL × 2 HEC HEME C × 2 BOG octyl beta-D-glucopyranoside × 5 FES FE2/S2 (INORGANIC) CLUSTER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.7；277 K；20MM KMES PH 6.7, 75MM NACL, 10% GLYCEROL, AND 6% PEG4000, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 3.16 Å R-free 0.291
3H1I Stigmatellin and antimycin bound cytochrome bc1 complex from chicken Deposited 2009-04-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain C 1–380（380 aa） Chain P 1–380（380 aa）	Not recorded	PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 UNL UNKNOWN LIGAND × 10 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 SMA STIGMATELLIN A × 2 ANY 2-METHYL-BUTYRIC ACID 3-(3-FORMYLAMINO-2-HYDROXY-BENZOYLAMINO)-8-HEPTYL-2,6-DIMETHYL-4,9-DIOXO-[1,5]DIOXONAN-7-YL ESTER × 2 CDL CARDIOLIPIN × 4 GOL GLYCEROL × 2 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PLC DIUNDECYL PHOSPHATIDYL CHOLINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.7；277 K；20MM KMES PH 6.7, 75MM NACL, 10% GLYCEROL, AND 6% PEG4000, INHIBITORS WERE ADDED FROM ETHANOLIC SOLUTION, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 3.53 Å R-free 0.306
3H1J Stigmatellin-bound cytochrome bc1 complex from chicken Deposited 2009-04-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain C 1–380（380 aa） Chain P 1–380（380 aa）	Not recorded	UNL UNKNOWN LIGAND × 10 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 SMA STIGMATELLIN A × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 FES FE2/S2 (INORGANIC) CLUSTER × 2 PLC DIUNDECYL PHOSPHATIDYL CHOLINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.7；277 K；20MM KMES PH 6.7, 75MM NACL, 10% GLYCEROL, AND 6% PEG4000, INHIBITOR WAS ADDED FROM ETHANOLIC SOLUTION, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 3.00 Å R-free 0.277
3H1K Chicken cytochrome BC1 complex with ZN++ and an iodinated derivative of kresoxim-methyl bound Deposited 2009-04-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain C 1–380（380 aa） Chain P 1–380（380 aa）	Not recorded	PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 UNL UNKNOWN LIGAND × 5 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 IKR methyl (2E)-{2-[(4-iodo-2,5-dimethylphenoxy)methyl]phenyl}(methoxyimino)ethanoate × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 CDL CARDIOLIPIN × 4 ZN ZINC ION × 2 GOL GLYCEROL × 2 HEC HEME C × 2 BOG octyl beta-D-glucopyranoside × 5 FES FE2/S2 (INORGANIC) CLUSTER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.7；277 K；20MM KMES PH 6.7, 75MM NACL, 10% GLYCEROL, AND 6% PEG4000. The Kresoxim-methyl derivative WAS ADDED to the protein FROM ETHANOLIC SOLUTION. After verifying good diffraction by these crystals, some were transferred to a drop of mother liquor supplemented with glycerol and ~0.2 mM ZnCl2. After 1 week this crystal was flash-cooled for data collection. During analysis of Zn binding presence of the inhibitor was overlooked, and in the primary citation publication the anomalous signal of I in the inhibitor was mistakenly attributed to a second Zn binding site, Zn02. VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 3.48 Å R-free 0.284
3H1L Chicken cytochrome BC1 complex with ascochlorin bound at QO and QI sites Deposited 2009-04-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain C 1–380（380 aa） Chain P 1–380（380 aa）	Not recorded	PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 UNL UNKNOWN LIGAND × 12 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 3H1 3-chloro-4,6-dihydroxy-2-methyl-5-{(2E,4E)-3-methyl-5-[(1R,2R,6R)-1,2,6-trimethyl-3-oxocyclohexyl]penta-2,4-dien-1-yl}benzaldehyde × 4 CDL CARDIOLIPIN × 4 GOL GLYCEROL × 2 HEC HEME C × 2 BOG octyl beta-D-glucopyranoside × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.77；277 K；Final concentrations before diffusion: 50 mM Cacodylate, 9.4 mM TrisHCl, 10 mM MgCl2, 50 g/L glycerol, 30 g/L PEG 3350Da, 0.23 mM EDTA, 0.47 g/L undecyl maltoside, 31 mM octyl glucoside, pH 6.77, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 3.21 Å R-free 0.295
3L70 Cytochrome BC1 complex from chicken with trifloxystrobin bound Deposited 2009-12-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain C 1–380（380 aa） Chain P 1–380（380 aa）	Not recorded	PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 JZV methyl (2E)-(methoxyimino)(2-{[({(1Z)-1-[3-(trifluoromethyl)phenyl]ethylidene}amino)oxy]methyl}phenyl)ethanoate × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 CDL CARDIOLIPIN × 4 GOL GLYCEROL × 2 HEC HEME C × 2 BOG octyl beta-D-glucopyranoside × 5 FES FE2/S2 (INORGANIC) CLUSTER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.77；277 K；FINAL CONCENTRATIONS BEFORE DIFFUSION: 50 MM CACODYLATE, 9.4 MM TRISHCL, 10 MM MGCL2, 50 G/L GLYCEROL, 30 G/L PEG 3350DA, 0.23 MM EDTA, 0.47 G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.75 Å R-free 0.297
3L71 Cytochrome BC1 complex from chicken with azoxystrobin bound Deposited 2009-12-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain C 1–380（380 aa） Chain P 1–380（380 aa）	Not recorded	PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 AZO METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 5 FES FE2/S2 (INORGANIC) CLUSTER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.77；277 K；FINAL CONCENTRATIONS BEFORE DIFFUSION: 50 MM CACODYLATE, 9.4 MM TRISHCL, 10 MM MGCL2, 50 G/L GLYCEROL, 30 G/L PEG 3350DA, 0.23 MM EDTA, 0.47 G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.84 Å R-free 0.281
3L72 Chicken cytochrome BC1 complex with kresoxim-I-dimethyl bound Deposited 2009-12-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain C 1–380（380 aa） Chain P 1–380（380 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 IKR methyl (2E)-{2-[(4-iodo-2,5-dimethylphenoxy)methyl]phenyl}(methoxyimino)ethanoate × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 CDL CARDIOLIPIN × 4 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 GOL GLYCEROL × 2 HEC HEME C × 2 BOG octyl beta-D-glucopyranoside × 5 FES FE2/S2 (INORGANIC) CLUSTER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.7；277 K；20MM KMES PH 6.7, 75MM NACL, 10% GLYCEROL, AND 6% PEG4000, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 3.06 Å R-free 0.294
3L73 Cytochrome BC1 complex from chicken with triazolone inhibitor Deposited 2009-12-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain C 1–380（380 aa） Chain P 1–380（380 aa）	Not recorded	PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 JZZ 4-[7-(3,3-dimethylbut-1-yn-1-yl)naphthalen-1-yl]-5-methoxy-2-methyl-2,4-dihydro-3H-1,2,4-triazol-3-one × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 5 FES FE2/S2 (INORGANIC) CLUSTER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.77；277 K；FINAL CONCENTRATIONS BEFORE DIFFUSION: 50 MM CACODYLATE, 9.4 MM TRISHCL, 10 MM MGCL2, 50 G/L GLYCEROL, 30 G/L PEG 3350DA, 0.23 MM EDTA, 0.47 G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 3.04 Å R-free 0.293
3L74 Cytochrome BC1 complex from chicken with famoxadone bound Deposited 2009-12-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain C 1–380（380 aa） Chain P 1–380（380 aa）	Not recorded	PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 UNL UNKNOWN LIGAND × 11 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 FMX FAMOXADONE × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 AZI AZIDE ION × 2 BOG octyl beta-D-glucopyranoside × 6 HEC HEME C × 2 CDL CARDIOLIPIN × 4 FES FE2/S2 (INORGANIC) CLUSTER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.77；273 K；FINAL CONCENTRATIONS BEFORE DIFFUSION: 50 MM CACODYLATE, 9.4 MM TRISHCL, 10 MM MGCL2, 50 G/L GLYCEROL, 30 G/L PEG 3350DA, 0.23 MM EDTA, 0.47 G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77 , VAPOR DIFFUSION, SITTING DROP, temperature 273K	Resolution 2.76 Å R-free 0.286
3L75 Cytochrome BC1 complex from chicken with fenamidone bound Deposited 2009-12-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain C 1–380（380 aa） Chain P 1–380（380 aa）	Not recorded	PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 UNL UNKNOWN LIGAND × 11 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 FNM (5S)-5-methyl-2-(methylsulfanyl)-5-phenyl-3-(phenylamino)-3,5-dihydro-4H-imidazol-4-one × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 AZI AZIDE ION × 2 BOG octyl beta-D-glucopyranoside × 6 HEC HEME C × 2 CDL CARDIOLIPIN × 4 FES FE2/S2 (INORGANIC) CLUSTER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.77；277 K；FINAL CONCENTRATIONS BEFORE DIFFUSION: 50 MM CACODYLATE, 9.4 MM TRISHCL, 10 MM MGCL2, 50 G/L GLYCEROL, 30 G/L PEG 3350DA, 0.23 MM EDTA, 0.47 G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.79 Å R-free 0.275
3TGU Cytochrome bc1 complex from chicken with pfvs-designed moa inhibitor bound Deposited 2011-08-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain C 2–380（379 aa） Chain P 2–380（379 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	UNL UNKNOWN LIGAND × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 WF3 methyl (2E)-3-methoxy-2-[2-({[6-methyl-3-(trifluoromethyl)quinoxalin-2-yl]oxy}methyl)phenyl]prop-2-enoate × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 CDL CARDIOLIPIN × 4 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 GOL GLYCEROL × 2 HEC HEME C × 2 BOG octyl beta-D-glucopyranoside × 5 FES FE2/S2 (INORGANIC) CLUSTER × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.77；278 K；50 mm cacodylate, 9.4 mM TrisHCl, 30 mM K-MES, 1.8 mM K-MOPS, 30 mM NaCl, 31 mM KCl, 10 mM MgCl2, 91 g/l glycerol, 30 g/l PEG 4kDa, 0.9 mM NaN3, 0.05 mM EDTA, 0.47g/l undecyl maltoside, 31 mM octyl glucoside, pH 6.77, VAPOR DIFFUSION, HANGING DROP, temperature 278K	Resolution 2.70 Å R-free 0.289
4U3F Cytochrome bc1 complex from chicken with designed inhibitor bound Deposited 2014-07-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain C 2–380（379 aa） Chain P 2–380（379 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 14 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 Y52 methyl (2E)-3-methoxy-2-(2-{[(5-methoxy-1,3-benzothiazol-2-yl)sulfanyl]methyl}phenyl)prop-2-enoate × 2 U10 UBIQUINONE-10 × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 3 FES FE2/S2 (INORGANIC) CLUSTER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.77；278 K；CRYSTALLIZATION CONDITIONS: 50 MM CACODYLATE, 9.4 MM TRISHCL, 30 MM K-MES, 1.8 MM K-MOPS, 30 MM NACL, 31 MM KCL, 10 MM MGCL2, 91 G/L GLYCEROL, 30 G/L PEG 4KDA, 0.9 MM NAN3, 0.05 MM EDTA, 0.47G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, TEMPERATURE 278K	Resolution 3.23 Å R-free 0.284

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CYB_CHICK
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–380； UniProt 1–380

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

暂无 SAXS 图

P(r) Distance Distribution P(r) Distribution

暂无 P(r) 图

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2bcc
Deposition date deposition_date	1998-09-18
Structure title title	STIGMATELLIN-BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN
Keywords keywords	UBIQUINONE, OXIDOREDUCTASE, REDOX ENZYME, MEMBRANE PROTEIN, RESPIRATORY CHAIN, STIGMATELLIN; OXIDOREDUCTASE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

该条目暂无 SAXS 数据。

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

该条目暂无 P(r) 分析数据。

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (16)

Entity 1 Entity 1 polymer

Description description	UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
Molecular weight formula_weight	49795.9 kDa
EC 编号 ec_number	1.10.2.2
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	15754

TAYYAQALQSVPETQVSQLDNGVRVASEQSSQPTCTVGVWIDAGSRYESEKNNGAGYFLEHLAFKGTKNRPQNALEKEVESMGAHLNAYSSREHTAYYIKALSKDVPKAVELLADIVQNCSLEDSQIEKERDVIVRELQENDTSMREVVFNYLHATAFQGTGLAQSVEGPSENIRKLSRADLTEYLSTHYTAPRMVLAAAGGVEHQQLLELAQKHFGGVPFTYDDDAVPTLSKCRFTGSQIRHREDGLPLAHVAIAVEGPGWAHPDLVALQVANAIIGHYDRTYGGGLHSSSPLASIAVTNKLCQSFQTFSICYSETGLFGFYFVCDRMSIDDMMFVLQGQWMRLCTSISESEVLRGKNFLRNALVSHLDGTTPVCEDIGRELLTYGRRIPLEEWEERLAEVDARMVREVCSKYIYDQCPAVAGPGPIEQLPDYNRIRSGMFWLRF

Entity 2 Entity 2 polymer

Description description	UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
Molecular weight formula_weight	45091.7 kDa
EC 编号 ec_number	1.10.2.2
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

PPHPQDLEITKLPNGLVIASLENYSPGSTIGVFIKAGSRYENSSNLGTSHLLRLASSLTTKGASSFKITRGIEAVGGKLSVESTRENMAYTVECLRDDVEILMEFLLNVTTAPEFRPWEVADLQPQLKIDKAVAFQNPQTHVIENLHAAAYRNALADSLYCPDYRIGKVTSVELHDFVQNHFTSARMALVGLGVSHPVLKNVAEQLLNIRGGLGLSGAKAKYRGGEIREQNGDSLVHAAIVAESAAIGGAEANAFSVLQHVLGANPHVKRGLNATSSLYQAVAKGVHQPFDVSAFNASYSDSGLFGFYTISQAAYAGQVIKAAYNQVKTIAQGNVSNENVQAAKNKLKAKYLMSVESSEGFLEEVGSQALAAGSYNPPSTVLQQIDAVADADVIKAAKKFVSRQKSMAASGNLGHTPFVDEL

Entity 3 Entity 3 polymer

Description description	UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
Molecular weight formula_weight	42623.0 kDa
EC 编号 ec_number	1.10.2.2
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

MAPNIRKSHPLLKMINNSLIDLPAPSNISAWWNFGSLLAVCLMTQILTGLLLAMHYTADTSLAFSSVAHTCRNVQYGWLIRNLHANGASFFFICIFLHIGRGLYYGSYLYKETWNTGVILLLTLMATAFVGYVLPWGQMSFWGATVITNLFSAIPYIGHTLVEWAWGGFSVDNPTLTRFFALHFLLPFAIAGITIIHLTFLHESGSNNPLGISSDSDKIPFHPYYSFKDILGLTLMLTPFLTLALFSPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAASVLILFLIPFLHKSKQRTMTFRPLSQTLFWLLVANLLILTWIGSQPVEHPFIIIGQMASLSYFTILLILFPTIGTLENKMLNY

Entity 4 Entity 4 polymer

Description description	UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
Molecular weight formula_weight	27357.2 kDa
EC 编号 ec_number	1.10.2.2
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D

SDLELHPPSYPWSHRGPLSSLDHTSIRRGFQVYKQVCSSCHSMDYVAYRHLVGVCYTEDEAKALAEEVEVQDGPNEDGEMFMRPGKLSDYFPKPYPNPEAARAANNGALPPDLSYIVRARHGGEDYVFSLLTGYCEPPTGVSVREGLYFNPYFPGQAIGMAPPIYNDVLEFDDGTPATMSQVAKDVCTFLRWAAEPEHDHRKRMGLKMLLMMGLLVPLVYYMKRHKWSVLKSRKLAYRPPK

Entity 5 Entity 5 polymer

Description description	UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
Molecular weight formula_weight	21739.7 kDa
EC 编号 ec_number	1.10.2.2
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E

SHTDIKVPNFSDYRRPPDDYSTKSSRESDPSRKGFSYLVTAVTTLGVAYAAKNVVTQFVSSMSASADVLAMSKIEIKLSDIPEGKNMAFKWRGKPLFVRHRTKKEIDQEAAVEVSQLRDPQHDLERVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPCHGSHYDASGRIRKGPAPLNLEVPSYEFTSDDMVIVG

Entity 6 Entity 6 polymer

Description description	UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
Molecular weight formula_weight	13400.1 kDa
EC 编号 ec_number	1.10.2.2
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F

AGRPAVSASSRWLEGIRKWYYNAAGFNKYGLMRDDTIYENDDVKEAIRRLPENLYDDRMFRIKRALDLNMRQQILPKEQWTKYEEDVPYLEPYLKEVIRERKEREEWDK

Entity 7 Entity 7 polymer

Description description	UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
Molecular weight formula_weight	9715.2 kDa
EC 编号 ec_number	1.10.2.2
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G

GRQFGHLTRVRHLITYSLSPFEQRPFPHYFSKGVPNVWRRLRACILRVAPPFLAFYLLYTWGTQEFEKSKRKNPAAYVNDR

Entity 8 Entity 8 polymer

Description description	UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
Molecular weight formula_weight	9223.1 kDa
EC 编号 ec_number	1.10.2.2
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

GDPKEEEEEEEELVDPLTTVREQCEQLEKCVKARERLELCDERVSSRSQTEEDCTEELFDFLHARDHCVAHKLFNSLK

Entity 9 Entity 9 polymer

Description description	UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
Molecular weight formula_weight	2826.5 kDa
EC 编号 ec_number	1.10.2.2
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I

XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

Entity 10 Entity 10 polymer

Description description	UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
Molecular weight formula_weight	7175.3 kDa
EC 编号 ec_number	1.10.2.2
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	J

VAPTLTARLYSLLFRRTSTFALTIVVGALLFERAFDQGADAIYEHINEGKLWKHIKHKYENK

Entity 11 Entity 11 non-polymer

Description description	PROTOPORPHYRIN IX CONTAINING FE
Molecular weight formula_weight	616.5 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 12 Entity 12 non-polymer

Description description	UBIQUINONE-10
Molecular weight formula_weight	863.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 13 Entity 13 non-polymer

Description description	1,2-dioleoyl-sn-glycero-3-phosphoethanolamine
Molecular weight formula_weight	744.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 14 Entity 14 non-polymer

Description description	STIGMATELLIN
Molecular weight formula_weight	482.7 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 15 Entity 15 non-polymer

Description description	octyl beta-D-glucopyranoside
Molecular weight formula_weight	292.4 kDa
Source method src_method	man
Copy count entity_count	1

Entity 16 Entity 16 non-polymer

Description description	FE2/S2 (INORGANIC) CLUSTER
Molecular weight formula_weight	175.8 kDa
Source method src_method	syn
Copy count entity_count	1

▼

7. Fold Classification (SCOP + CATH) 27 domains

SCOP 2.08 (14 domains)

Domain ID domain_id	d2bcca1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d2bcca2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d2bccb1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d2bccb2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d2bccc2
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.32 — a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Superfamily Superfamily superfamily	f.32.1 — a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family family	f.32.1.1 — a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)

Domain ID domain_id	d2bccc3
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.21 — Heme-binding four-helical bundle
Superfamily Superfamily superfamily	f.21.1 — Transmembrane di-heme cytochromes
Family Family family	f.21.1.2 — Cytochrome b of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)

Domain ID domain_id	d2bccd2
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.3 — Cytochrome bc1 domain

Domain ID domain_id	d2bccd3
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.23 — Single transmembrane helix
Superfamily Superfamily superfamily	f.23.11 — Cytochrome c1 subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase), transmembrane anchor
Family Family family	f.23.11.1 — Cytochrome c1 subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase), transmembrane anchor

Domain ID domain_id	d2bcce1
Class class	b — All beta proteins
Fold Fold fold	b.33 — ISP domain
Superfamily Superfamily superfamily	b.33.1 — ISP domain
Family Family family	b.33.1.1 — Rieske iron-sulfur protein (ISP)

Domain ID domain_id	d2bcce2
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.23 — Single transmembrane helix
Superfamily Superfamily superfamily	f.23.12 — ISP transmembrane anchor
Family Family family	f.23.12.1 — ISP transmembrane anchor

Domain ID domain_id	d2bccf_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.27 — 14 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Superfamily Superfamily superfamily	f.27.1 — 14 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family family	f.27.1.1 — 14 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)

Domain ID domain_id	d2bccg_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.23 — Single transmembrane helix
Superfamily Superfamily superfamily	f.23.13 — Ubiquinone-binding protein QP-C of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family family	f.23.13.1 — Ubiquinone-binding protein QP-C of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)

Domain ID domain_id	d2bcch_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.28 — Non-heme 11 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Superfamily Superfamily superfamily	f.28.1 — Non-heme 11 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family family	f.28.1.1 — Non-heme 11 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)

Domain ID domain_id	d2bccj_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.23 — Single transmembrane helix
Superfamily Superfamily superfamily	f.23.14 — Subunit X (non-heme 7 kDa protein) of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family family	f.23.14.1 — Subunit X (non-heme 7 kDa protein) of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)

CATH v4.4 (13 domains)

Domain ID domain_id	2bccA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	2bccA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	2bccB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	2bccB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	2bccC00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	810 — Cytochrome Bc1 Complex; Chain C
Homologous superfamily homologous superfamily	10 — Cytochrome Bc1 Complex; Chain C

Domain ID domain_id	2bccD01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	100 — Cytochrome c1, transmembrane anchor, C-terminal

Domain ID domain_id	2bccD02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	2bccE01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	270 — Ubiquinol cytochrome reductase, transmembrane domain

Domain ID domain_id	2bccE02
Class class	2 — Mainly Beta
Architecture architecture	102 — 3-layer Sandwich
Topology topology	10 — Rieske Iron-sulfur Protein
Homologous superfamily homologous superfamily	10 — Rieske [2Fe-2S] iron-sulphur domain

Domain ID domain_id	2bccF00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1090 — Cytochrome Bc1 Complex; Chain F
Homologous superfamily homologous superfamily	10 — Cytochrome b-c1 complex subunit 7

Domain ID domain_id	2bccG00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	210 — Cytochrome b-c1 complex subunit 8

Domain ID domain_id	2bccH00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	20 — Ubiquinol-cytochrome C reductase hinge domain

Domain ID domain_id	2bccJ00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	260 — Cytochrome b-c1 complex subunit 9

▶

8. Citations (2)

▶

Unit-cell length a length_a	173.460 Å
Unit-cell length b length_b	182.450 Å
Unit-cell length c length_c	241.330 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	3.500 Å
Low-resolution limit resolution_low	12.000 Å
R factor r_factor	0.2840
R_work r_work	0.2840
R_free r_free	0.3170

STIGMATELLIN-BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN

1. Protein Identity and Related Structures Protein Identity & Related Structures

UBIQUINOL CYTOCHROME C OXIDOREDUCTASE

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (16)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 polymer

Polymer Polymer

Entity 6 Entity 6 polymer

Polymer Polymer

Entity 7 Entity 7 polymer

Polymer Polymer

Entity 8 Entity 8 polymer

Polymer Polymer

Entity 9 Entity 9 polymer

Polymer Polymer

Entity 10 Entity 10 polymer

Polymer Polymer

Entity 11 Entity 11 non-polymer

Entity 12 Entity 12 non-polymer

Entity 13 Entity 13 non-polymer

Entity 14 Entity 14 non-polymer

Entity 15 Entity 15 non-polymer

Entity 16 Entity 16 non-polymer

7. Fold Classification (SCOP + CATH) 27 domains

SCOP 2.08 (14 domains)

CATH v4.4 (13 domains)

8. Citations (2)

9. Files and Curves (0)