8gt0

Structure of falcipain and human Stefin A complex

Method: X-RAY DIFFRACTION D_max: 107.8 Å Quality: REASONABLE

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

Cysteine protease falcipain-2

Plasmodium falciparum

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 244–484	Not recorded	Cystatin-A × 1 （P01040） GOL GLYCEROL × 38 NA SODIUM ION × 10 PEG DI(HYDROXYETHYL)ETHER × 9 PE8 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL × 8 EDO 1,2-ETHANEDIOL × 7 PG4 TETRAETHYLENE GLYCOL × 16 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；290 K；0.05 M cadmium chloride, 0.1 M Na HEPES pH 7.5, 1.0 M sodium acetate and 5 mM MgSO4	Resolution 3.28 Å R-free 0.299
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 244–484	Not recorded	Cystatin-A × 1 （P01040） GOL GLYCEROL × 23 NA SODIUM ION × 13 PEG DI(HYDROXYETHYL)ETHER × 11 PE8 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL × 2 EDO 1,2-ETHANEDIOL × 4 PG4 TETRAETHYLENE GLYCOL × 14 SO4 SULFATE ION × 5 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；290 K；0.05 M cadmium chloride, 0.1 M Na HEPES pH 7.5, 1.0 M sodium acetate and 5 mM MgSO4	Resolution 3.28 Å R-free 0.299
3	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain E； UniProt 244–484	Not recorded	GOL GLYCEROL × 3 NA SODIUM ION × 2 PEG DI(HYDROXYETHYL)ETHER × 4 PE8 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL × 3 PG4 TETRAETHYLENE GLYCOL × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；290 K；0.05 M cadmium chloride, 0.1 M Na HEPES pH 7.5, 1.0 M sodium acetate and 5 mM MgSO4	Resolution 3.28 Å R-free 0.299

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 8GT0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6JW9 Crystal structure of E-64 inhibited falcipain 2 from Plasmodium falciparum, strain 3D7 Deposited 2019-04-18	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 244–484（241 aa）	Not recorded	E64 N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；293 K；0.4 M Ammonium Sulfate, 0.1 M Sodium Citrate, 25% Ethylene Glycol, 5 mM MgSO4	Resolution 3.50 Å R-free 0.328
6JW9 Crystal structure of E-64 inhibited falcipain 2 from Plasmodium falciparum, strain 3D7 Deposited 2019-04-18	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 244–484（241 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；293 K；0.4 M Ammonium Sulfate, 0.1 M Sodium Citrate, 25% Ethylene Glycol, 5 mM MgSO4	Resolution 3.50 Å R-free 0.328
7EI0 Crystal structure of falcipain 2 from 3D7 strain Deposited 2021-03-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 244–484（241 aa） Chain B 244–484（241 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	PGE TRIETHYLENE GLYCOL × 4 SO4 SULFATE ION × 2 EDO 1,2-ETHANEDIOL × 3 NA SODIUM ION × 2 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；300 K；ethylene glycol, ammonium sulfate	Resolution 3.40 Å R-free 0.285
8GT7 Structure of falcipain and human Stefin A mutant complex Deposited 2022-09-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 244–484（241 aa） Chain C 244–484（241 aa）	Not recorded	GOL GLYCEROL × 65 NA SODIUM ION × 44 PG4 TETRAETHYLENE GLYCOL × 48 SO4 SULFATE ION × 5 PEG DI(HYDROXYETHYL)ETHER × 54 PE8 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL × 12 EDO 1,2-ETHANEDIOL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；290 K；0.05 M cadmium chloride, 0.1 M Na HEPES pH 7.5 and 1.5 M sodium acetate	Resolution 3.28 Å R-free 0.300

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q8I6U4_PLAF7
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–241； UniProt 244–484 Author chain C； PDBConstruct 1–241； UniProt 244–484 Author chain E； PDBConstruct 1–241； UniProt 244–484

Cystatin-A

Homo sapiens

UniProt P01040

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 1–98	Not recorded	Cysteine protease falcipain-2 × 1 （Q8I6U4） GOL GLYCEROL × 38 NA SODIUM ION × 10 PEG DI(HYDROXYETHYL)ETHER × 9 PE8 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL × 8 EDO 1,2-ETHANEDIOL × 7 PG4 TETRAETHYLENE GLYCOL × 16 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；290 K；0.05 M cadmium chloride, 0.1 M Na HEPES pH 7.5, 1.0 M sodium acetate and 5 mM MgSO4	Resolution 3.28 Å R-free 0.299
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 1–98	Not recorded	Cysteine protease falcipain-2 × 1 （Q8I6U4） GOL GLYCEROL × 23 NA SODIUM ION × 13 PEG DI(HYDROXYETHYL)ETHER × 11 PE8 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL × 2 EDO 1,2-ETHANEDIOL × 4 PG4 TETRAETHYLENE GLYCOL × 14 SO4 SULFATE ION × 5 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；290 K；0.05 M cadmium chloride, 0.1 M Na HEPES pH 7.5, 1.0 M sodium acetate and 5 mM MgSO4	Resolution 3.28 Å R-free 0.299

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 8GT0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CYU SOLUTION NMR STRUCTURE OF RECOMBINANT HUMAN CYSTATIN A UNDER THE CONDITION OF PH 3.8 AND 310K Deposited 1995-08-24	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–98（98 aa）	Mutation：DEL(M1), M65L	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1CYV SOLUTION NMR STRUCTURE OF RECOMBINANT HUMAN CYSTATIN A UNDER THE CONDITION OF PH 3.8 AND 310K Deposited 1995-08-24	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–98（98 aa）	Mutation：DEL(M1), M65L	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1DVC SOLUTION NMR STRUCTURE OF HUMAN STEFIN A AT PH 5.5 AND 308K, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1996-02-26	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–98（98 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；308 K	Resolution not provided
1DVD SOLUTION NMR STRUCTURE OF HUMAN STEFIN A AT PH 5.5 AND 308K, NMR, 17 STRUCTURES Deposited 1996-02-26	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–98（98 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；308 K	Resolution not provided
1GD3 refined solution structure of human cystatin A Deposited 2000-09-08	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–98（98 aa）	Mutation：M65L	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；310 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 1.4mM cystatin A U-15N,13C; 10mM Acetate buffer NA; 95% H2O, 5% D2O \| 95% H2O/5% D2O NMR sample composition 1.4mM cystatin A U-15N; 10mM Acetate buffer NA; 95% H2O, 5% D2O \| 95% H2O/5% D2O NMR sample composition 1.4mM cystatin A; 10mM Acetate buffer NA; 98% D2O \| 98% D2O	Resolution not provided
1GD4 SOLUTION STRUCTURE OF P25S CYSTATIN A Deposited 2000-09-08	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–98（98 aa）	Mutation：M65L,P25S	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；310 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 1.4mM P25S cystatin A U-15N,13C; 10mM Acetate buffer ; 95% H2O, 5% D2O \| 95% H2O/5% D2O NMR sample composition 1.4mM P25S cystatin A U-15N; 10mM Acetate buffer ; 90% H2O 10% D2O \| 95% H2O/5% D2O NMR sample composition 1.4mM P25S cystatin A; 10mM Acetate buffer ; 98% D2O \| 98% D2O	Resolution not provided
1N9J Solution Structure of the 3D domain swapped dimer of Stefin A Deposited 2002-11-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–98（98 aa） Chain B 1–98（98 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；308 K；Pressure ambient NMR sample composition 1.2mM Stefin A U-15N; 50mM phosphate buffer pH 5.5, 100mM KCl, 5mM Azide; 90% H2O, 10% D2O \| 90% H2O/10% D2O NMR sample composition 1mM Stefin A U-15N,13C,2H; 50mM phosphate buffer pH 5.5, 100mM KCl, 5mM Azide; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
1NB3 Crystal structure of stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo-and exopeptidases Deposited 2002-12-02	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain I 1–98（98 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å R-free 0.246
1NB3 Crystal structure of stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo-and exopeptidases Deposited 2002-12-02	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain J 1–98（98 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å R-free 0.246
1NB3 Crystal structure of stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo-and exopeptidases Deposited 2002-12-02	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain K 1–98（98 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å R-free 0.246
1NB3 Crystal structure of stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo-and exopeptidases Deposited 2002-12-02	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain L 1–98（98 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å R-free 0.246
1NB5 Crystal structure of stefin A in complex with cathepsin H Deposited 2002-12-02	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain I 1–98（98 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.2；298 K；PEG 4000, ammonium sulphate, sodium acetate, cadmium chloride, pH 4.2, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.40 Å R-free 0.274
1NB5 Crystal structure of stefin A in complex with cathepsin H Deposited 2002-12-02	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain J 1–98（98 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.2；298 K；PEG 4000, ammonium sulphate, sodium acetate, cadmium chloride, pH 4.2, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.40 Å R-free 0.274
1NB5 Crystal structure of stefin A in complex with cathepsin H Deposited 2002-12-02	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain K 1–98（98 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.2；298 K；PEG 4000, ammonium sulphate, sodium acetate, cadmium chloride, pH 4.2, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.40 Å R-free 0.274
1NB5 Crystal structure of stefin A in complex with cathepsin H Deposited 2002-12-02	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain L 1–98（98 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.2；298 K；PEG 4000, ammonium sulphate, sodium acetate, cadmium chloride, pH 4.2, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.40 Å R-free 0.274
3K9M Cathepsin B in complex with stefin A Deposited 2009-10-16	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–98（98 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.2M ammonium suphate, 24% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.61 Å R-free 0.250
3K9M Cathepsin B in complex with stefin A Deposited 2009-10-16	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–98（98 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.2M ammonium suphate, 24% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.61 Å R-free 0.250
3KFQ Unreduced cathepsin V in complex with stefin A Deposited 2009-10-27	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–98（98 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；0.1M Tris-HCl, 12% PEG3000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.99 Å R-free 0.219
3KFQ Unreduced cathepsin V in complex with stefin A Deposited 2009-10-27	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–98（98 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；0.1M Tris-HCl, 12% PEG3000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.99 Å R-free 0.219
3KSE Unreduced cathepsin L in complex with stefin A Deposited 2009-11-22	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–98（98 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；0.1M Tris-HCl, 16% PEG3000, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.71 Å R-free 0.204
3KSE Unreduced cathepsin L in complex with stefin A Deposited 2009-11-22	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1–98（98 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；0.1M Tris-HCl, 16% PEG3000, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.71 Å R-free 0.204
3KSE Unreduced cathepsin L in complex with stefin A Deposited 2009-11-22	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 1–98（98 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；0.1M Tris-HCl, 16% PEG3000, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.71 Å R-free 0.204
8GT7 Structure of falcipain and human Stefin A mutant complex Deposited 2022-09-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 1–98（98 aa） Chain D 1–98（98 aa）	Mutation：K68R Mutation：K68R	GOL GLYCEROL × 65 NA SODIUM ION × 44 PG4 TETRAETHYLENE GLYCOL × 48 SO4 SULFATE ION × 5 PEG DI(HYDROXYETHYL)ETHER × 54 PE8 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL × 12 EDO 1,2-ETHANEDIOL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；290 K；0.05 M cadmium chloride, 0.1 M Na HEPES pH 7.5 and 1.5 M sodium acetate	Resolution 3.28 Å R-free 0.300

13 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CYTA_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–98； UniProt 1–98 Author chain D； PDBConstruct 1–98； UniProt 1–98

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

P(r) Distance Distribution P(r) Distribution

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

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	8gt0
Deposition date deposition_date	2022-09-07
Structure title title	Structure of falcipain and human Stefin A complex
Keywords keywords	falcipain, stefin, complex, HYDROLASE; HYDROLASE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	31.71 Å
Radius of gyration Rg (electron density) rg_electron	31.42 Å
Forward intensity I(0) i0	146630000.00
Molecular weight molecular_weight	99533.0 kDa
Excluded volume excluded_volume	126450 Å³
Envelope volume envelope_volume	183460 Å³
Hydration-shell volume shell_volume	47263 Å³
Envelope diameter envelope_diameter	115.3 Å
Shell Rg shell_rg	39.14 Å
Envelope Rg envelope_rg	32.20 Å
Shape Rg shape_rg	31.26 Å
Total Rg total_rg	32.71 Å
Total atoms total_atoms	6888
Residues n_residues	696
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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

Maximum dimension Dmax dmax	107.8 Å
Rg (real space) rg_real	31.65 Å
Rg uncertainty (real space) rg_real_error	0.90 Å
I(0) (real space) i0_real	1.4660e+08
I(0) uncertainty (real space) i0_real_error	2.2830e+06
Rg (reciprocal space) rg_reciprocal	31.68 Å
I(0) (reciprocal space) i0_reciprocal	146600000.0000
Solution quality estimate total_estimate	0.6621
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	38.8 Å
Skewness Skewness skewness	0.321
Kurtosis Kurtosis kurtosis	-0.292
Angular range angular_range	— – 0.2500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	58800000.0000
Real-space data points n_real_points	51
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.818; Stabil: 1.000; Sysdev: 0.062; Positv: 1.000; Valcen: 1.000; Smooth: 0.963

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (11)

Entity 1 Entity 1 polymer

Description description	Cysteine protease falcipain-2
Molecular weight formula_weight	27205.7 kDa
EC 编号 ec_number	3.4.22.-
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,E
Atom count atom_count	7032

QMNYEEVIKKYKGNENFDHAAYDWRLHSGVTPVKDQKNCGSCWAFSSIGSVESQYAIRKNKLITLSEQELVDCSFKNYGCNGGLINNAFEDMIELGGICTDDDYPYVSDAPNLCNIDRCTEKYGIKNYLSVPDNKLKEALRFLGPISISVAVSDDFAFYKEGIFDGECGDQLNHAVMLVGFGMKEIVNPLTKKGEKHYYYIIKNSWGQQWGERGFINIETDESGLMRKCGLGTDAFIPLIE

来源 Source

来源生物 organism	Plasmodium falciparum
通用名 common_name	malaria parasite P. falciparum
NCBI Class编号 ncbi_taxonomy_id	5833
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Cystatin-A
Molecular weight formula_weight	11020.5 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D

MIPGGLSEAKPATPEIQEIVDKVKPQLEEKTNETYGKLEAVQYKTQVVAGTNYYIKVRAGDNKYMHLKVFKSLPGQNEDLVLTGYQVDKNKDDELTGF

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	64

Entity 4 Entity 4 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	25

Entity 5 Entity 5 non-polymer

Description description	DI(HYDROXYETHYL)ETHER
Molecular weight formula_weight	106.1 kDa
Source method src_method	syn
Copy count entity_count	24

Entity 6 Entity 6 non-polymer

Description description	3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL
Molecular weight formula_weight	370.4 kDa
Source method src_method	syn
Copy count entity_count	13

Entity 7 Entity 7 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	11

Entity 8 Entity 8 non-polymer

Description description	TETRAETHYLENE GLYCOL
Molecular weight formula_weight	194.2 kDa
Source method src_method	syn
Copy count entity_count	31

Entity 9 Entity 9 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	7

Entity 10 Entity 10 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 11 Entity 11 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	144

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	8gt0A01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	70 — Cathepsin B; Chain A
Homologous superfamily homologous superfamily	10 — Cysteine proteinases

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8. Citations (1)

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Unit-cell length a length_a	65.100 Å
Unit-cell length b length_b	118.063 Å
Unit-cell length c length_c	119.340 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	12

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

Resolution resolution	3.280 Å
Low-resolution limit resolution_low	43.990 Å
R factor r_factor	0.2794
R_work r_work	0.2783
R_free r_free	0.2993

fit	/app/data/saxs_computation/gt/8gt0/8gt0.fit
pddf	/app/data/pr_computation/gt/8gt0/8gt0.pr.out
profile	/app/data/saxs_computation/gt/8gt0/8gt0.dat

Structure of falcipain and human Stefin A complex

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

Cysteine protease falcipain-2

State in the Current Structure

Other States of the Same Protein in the Database

Cystatin-A

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 (11)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

Entity 10 Entity 10 non-polymer

Entity 11 Entity 11 water

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)