SAXSdb — 7e5b

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

Apoptosis-associated speck-like protein containing a CARD

Homo sapiens

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 D； UniProt 1–91	Fragment：PYD Domain	Repebody (Rb-B7) × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.5；290 K；0.2M Ammonium Sulfate, 0.1M Bis-Tris:HCl pH 5.5, 25% (w/v) PEG 3350, 0.1M TCEP hydrochloride	Resolution 2.29 Å R-free 0.236
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 1–91	Fragment：PYD Domain	Repebody (Rb-B7) × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.5；290 K；0.2M Ammonium Sulfate, 0.1M Bis-Tris:HCl pH 5.5, 25% (w/v) PEG 3350, 0.1M TCEP hydrochloride	Resolution 2.29 Å R-free 0.236

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 7E5B	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1UCP NMR structure of the PYRIN domain of human ASC Deposited 2003-04-16	Different construct 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 1–91（91 aa） Fragment：PYRIN DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.7；301 K；Ionic strength (raw mmCIF value) 50mM；Pressure ambient NMR sample composition 1mM PYRIN domain \| 90% H2O/10% D2O NMR sample composition 1mM PYRIN domain \| 100% D2O	Resolution not provided
2KN6 Structure of full-length human ASC (Apoptosis-associated speck-like protein containing a CARD) Deposited 2009-08-16	Different construct 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 1–195（195 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.8；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 0.2mM [U-100% 13C; U-100% 15N] Apoptosis-associated speck-like protein containing a CARD-1, 0.1mM sodium azide-2, 5mM [U-2H] TCEP-3, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.2mM [U-15N] Apoptosis-associated speck-like protein containing a CARD-4, 0.1mM sodium azide-5, 5mM TCEP-6, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.2mM [U-13C; U-15N] Apoptosis-associated speck-like protein containing a CARD-7, 0.1mM sodium azide-8, 5mM [U-2H] TCEP-9, 100% D2O \| 100% D2O	Resolution not provided
3J63 Unified assembly mechanism of ASC-dependent inflammasomes Deposited 2013-12-05	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 × 15 PDB declaration: pentadecameric	Chain A 1–91（91 aa） Fragment：pyrin domain (UNP residues 1-91) Chain B 1–91（91 aa） Fragment：pyrin domain (UNP residues 1-91) Chain C 1–91（91 aa） Fragment：pyrin domain (UNP residues 1-91) Chain D 1–91（91 aa） Fragment：pyrin domain (UNP residues 1-91) Chain E 1–91（91 aa） Fragment：pyrin domain (UNP residues 1-91) Chain F 1–91（91 aa） Fragment：pyrin domain (UNP residues 1-91) Chain G 1–91（91 aa） Fragment：pyrin domain (UNP residues 1-91) Chain H 1–91（91 aa） Fragment：pyrin domain (UNP residues 1-91) Chain I 1–91（91 aa） Fragment：pyrin domain (UNP residues 1-91) Chain J 1–91（91 aa） Fragment：pyrin domain (UNP residues 1-91) Chain K 1–91（91 aa） Fragment：pyrin domain (UNP residues 1-91) Chain L 1–91（91 aa） Fragment：pyrin domain (UNP residues 1-91) Chain M 1–91（91 aa） Fragment：pyrin domain (UNP residues 1-91) Chain N 1–91（91 aa） Fragment：pyrin domain (UNP residues 1-91) Chain O 1–91（91 aa） Fragment：pyrin domain (UNP residues 1-91)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM vitrification conditions Cryogen ETHANE；Plunged into liquid ethane (FEI VITROBOT MARK IV)	Resolution 3.80 Å
5H8O Crystal structure of an ASC-binding nanobody in complex with the CARD domain of ASC Deposited 2015-12-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 115–195（81 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 3.5；291 K；0.1 M citric acid at pH 3.5 and 3 M sodium chloride	Resolution 4.21 Å R-free 0.356
6K99 Structure of ASC CARD filament Deposited 2019-06-14	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 × 12 PDB declaration: dodecameric	Chain A 112–194（83 aa） Chain B 112–194（83 aa） Chain C 112–194（83 aa） Chain D 112–194（83 aa） Chain E 112–194（83 aa） Chain F 112–194（83 aa） Chain G 112–194（83 aa） Chain H 112–194（83 aa） Chain I 112–194（83 aa） Chain J 112–194（83 aa） Chain K 112–194（83 aa） Chain L 112–194（83 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.10 Å R-free 0.226
6KI0 Crystal Structure of Human ASC-CARD Deposited 2019-07-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 112–195（84 aa） Fragment：caspase recruitment domain	Mutation：D108A,K109A,E198A,N199A,K265A	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291.15 K；1.80 M Ammonium Sulfate, 0.1 M HEPES 7.0	Resolution 2.00 Å R-free 0.252
6KI0 Crystal Structure of Human ASC-CARD Deposited 2019-07-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain B 112–195（84 aa） Fragment：caspase recruitment domain	Mutation：D108A,K109A,E198A,N199A,K265A	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291.15 K；1.80 M Ammonium Sulfate, 0.1 M HEPES 7.0	Resolution 2.00 Å R-free 0.252
6N1H Cryo-EM structure of ASC-CARD filament Deposited 2018-11-08	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 × 16 PDB declaration: hexadecameric	Chain A 112–194（83 aa） Fragment：CARD (UNP residues 112-194) Chain B 112–194（83 aa） Fragment：CARD (UNP residues 112-194) Chain C 112–194（83 aa） Fragment：CARD (UNP residues 112-194) Chain D 112–194（83 aa） Fragment：CARD (UNP residues 112-194) Chain E 112–194（83 aa） Fragment：CARD (UNP residues 112-194) Chain F 112–194（83 aa） Fragment：CARD (UNP residues 112-194) Chain G 112–194（83 aa） Fragment：CARD (UNP residues 112-194) Chain H 112–194（83 aa） Fragment：CARD (UNP residues 112-194) Chain I 112–194（83 aa） Fragment：CARD (UNP residues 112-194) Chain J 112–194（83 aa） Fragment：CARD (UNP residues 112-194) Chain K 112–194（83 aa） Fragment：CARD (UNP residues 112-194) Chain L 112–194（83 aa） Fragment：CARD (UNP residues 112-194) Chain M 112–194（83 aa） Fragment：CARD (UNP residues 112-194) Chain N 112–194（83 aa） Fragment：CARD (UNP residues 112-194) Chain O 112–194（83 aa） Fragment：CARD (UNP residues 112-194) Chain P 112–194（83 aa） Fragment：CARD (UNP residues 112-194)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.17 Å
7KEU Cryo-EM structure of the Caspase-1-CARD:ASC-CARD octamer Deposited 2020-10-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 113–194（82 aa） Fragment：UNP residues 113-194 Chain B 113–194（82 aa） Fragment：UNP residues 113-194 Chain C 113–194（82 aa） Fragment：UNP residues 113-194 Chain D 113–194（82 aa） Fragment：UNP residues 113-194	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
9WZ4 Full-length ASC-PYD filament Deposited 2025-09-29	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 × 14 PDB declaration: tetradecameric	Chain A 1–195（195 aa） Chain B 1–195（195 aa） Chain C 1–195（195 aa） Chain D 1–195（195 aa） Chain E 1–195（195 aa） Chain F 1–195（195 aa） Chain G 1–195（195 aa） Chain H 1–195（195 aa） Chain I 1–195（195 aa） Chain J 1–195（195 aa） Chain K 1–195（195 aa） Chain L 1–195（195 aa） Chain M 1–195（195 aa） Chain N 1–195（195 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.21 Å
9WZ5 Full-length ASC-CARD filament Deposited 2025-09-29	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 × 12 PDB declaration: dodecameric	Chain A 1–195（195 aa） Chain B 1–195（195 aa） Chain C 1–195（195 aa） Chain D 1–195（195 aa） Chain E 1–195（195 aa） Chain F 1–195（195 aa） Chain G 1–195（195 aa） Chain H 1–195（195 aa） Chain I 1–195（195 aa） Chain J 1–195（195 aa） Chain K 1–195（195 aa） Chain L 1–195（195 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.91 Å
9WZ7 Full-length ASCb filament Deposited 2025-09-29	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 × 14 PDB declaration: tetradecameric	Chain A 1–176（176 aa） Chain B 1–176（176 aa） Chain C 1–176（176 aa） Chain D 1–176（176 aa） Chain E 1–176（176 aa） Chain F 1–176（176 aa） Chain G 1–176（176 aa） Chain H 1–176（176 aa） Chain I 1–176（176 aa） Chain J 1–176（176 aa） Chain K 1–176（176 aa） Chain L 1–176（176 aa） Chain M 1–176（176 aa） Chain N 1–176（176 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.66 Å
9WZ8 Full-length ASC-GFP PYD-filament Deposited 2025-09-29	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 × 14 PDB declaration: tetradecameric	Chain A 1–195（195 aa） Chain B 1–195（195 aa） Chain C 1–195（195 aa） Chain D 1–195（195 aa） Chain E 1–195（195 aa） Chain F 1–195（195 aa） Chain G 1–195（195 aa） Chain H 1–195（195 aa） Chain I 1–195（195 aa） Chain J 1–195（195 aa） Chain K 1–195（195 aa） Chain L 1–195（195 aa） Chain M 1–195（195 aa） Chain N 1–195（195 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.14 Å
9WZB K21E/K22E-ASC CARD filament Deposited 2025-09-29	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 × 12 PDB declaration: dodecameric	Chain A 1–195（195 aa） Chain B 1–195（195 aa） Chain C 1–195（195 aa） Chain D 1–195（195 aa） Chain E 1–195（195 aa） Chain F 1–195（195 aa） Chain G 1–195（195 aa） Chain H 1–195（195 aa） Chain I 1–195（195 aa） Chain J 1–195（195 aa） Chain K 1–195（195 aa） Chain L 1–195（195 aa）	Mutation：K21E,K22E Mutation：K21E,K22E Mutation：K21E,K22E Mutation：K21E,K22E Mutation：K21E,K22E Mutation：K21E,K22E Mutation：K21E,K22E Mutation：K21E,K22E Mutation：K21E,K22E Mutation：K21E,K22E Mutation：K21E,K22E Mutation：K21E,K22E	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.67 Å
9WZC R41E-ASC CARD filament Deposited 2025-09-29	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 × 12 PDB declaration: dodecameric	Chain A 1–195（195 aa） Chain B 1–195（195 aa） Chain C 1–195（195 aa） Chain D 1–195（195 aa） Chain E 1–195（195 aa） Chain F 1–195（195 aa） Chain G 1–195（195 aa） Chain H 1–195（195 aa） Chain I 1–195（195 aa） Chain J 1–195（195 aa） Chain K 1–195（195 aa） Chain L 1–195（195 aa）	Mutation：R41E Mutation：R41E Mutation：R41E Mutation：R41E Mutation：R41E Mutation：R41E Mutation：R41E Mutation：R41E Mutation：R41E Mutation：R41E Mutation：R41E Mutation：R41E	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.45 Å
9WZD R125E-ASC PYD filament Deposited 2025-09-29	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 × 14 PDB declaration: tetradecameric	Chain A 1–195（195 aa） Chain B 1–195（195 aa） Chain C 1–195（195 aa） Chain D 1–195（195 aa） Chain E 1–195（195 aa） Chain F 1–195（195 aa） Chain G 1–195（195 aa） Chain H 1–195（195 aa） Chain I 1–195（195 aa） Chain J 1–195（195 aa） Chain K 1–195（195 aa） Chain L 1–195（195 aa） Chain M 1–195（195 aa） Chain N 1–195（195 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å
9WZG Full-length ASC-PYD filament Deposited 2025-09-29	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 × 14 PDB declaration: tetradecameric	Chain A 1–195（195 aa） Chain B 1–195（195 aa） Chain C 1–195（195 aa） Chain D 1–195（195 aa） Chain E 1–195（195 aa） Chain F 1–195（195 aa） Chain G 1–195（195 aa） Chain H 1–195（195 aa） Chain I 1–195（195 aa） Chain J 1–195（195 aa） Chain K 1–195（195 aa） Chain L 1–195（195 aa） Chain M 1–195（195 aa） Chain N 1–195（195 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.41 Å
9WZH Full-length ASC-CARD filament Deposited 2025-09-29	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 × 12 PDB declaration: dodecameric	Chain A 1–195（195 aa） Chain B 1–195（195 aa） Chain C 1–195（195 aa） Chain D 1–195（195 aa） Chain E 1–195（195 aa） Chain F 1–195（195 aa） Chain G 1–195（195 aa） Chain H 1–195（195 aa） Chain I 1–195（195 aa） Chain J 1–195（195 aa） Chain K 1–195（195 aa） Chain L 1–195（195 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.02 Å

17 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ASC_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 2–92； UniProt 1–91 Author chain D； PDBConstruct 2–92； UniProt 1–91

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	7e5b
Deposition date deposition_date	2021-02-18
Structure title title	Crystal structure of ASC PYD Domain and Rb-B7
Keywords keywords	Inflammasome, Apoptosis, PROTEIN BINDING; PROTEIN BINDING
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	28.80 Å
Radius of gyration Rg (electron density) rg_electron	27.71 Å
Forward intensity I(0) i0	93116800.00
Molecular weight molecular_weight	76515.0 kDa
Excluded volume excluded_volume	96182 Å³
Envelope volume envelope_volume	118450 Å³
Hydration-shell volume shell_volume	34723 Å³
Envelope diameter envelope_diameter	97.0 Å
Shell Rg shell_rg	35.91 Å
Envelope Rg envelope_rg	27.45 Å
Shape Rg shape_rg	27.69 Å
Total Rg total_rg	28.62 Å
Total atoms total_atoms	5393
Residues n_residues	712
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	90.0 Å
Rg (real space) rg_real	28.66 Å
Rg uncertainty (real space) rg_real_error	0.46 Å
I(0) (real space) i0_real	9.3120e+07
I(0) uncertainty (real space) i0_real_error	1.1500e+06
Rg (reciprocal space) rg_reciprocal	28.72 Å
I(0) (reciprocal space) i0_reciprocal	93120000.0000
Solution quality estimate total_estimate	0.9063
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	39.3 Å
Skewness Skewness skewness	0.110
Kurtosis Kurtosis kurtosis	-0.568
Angular range angular_range	— – 0.2750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	20650000.0000
Real-space data points n_real_points	56
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.934; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.979

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Repebody (Rb-B7)
Molecular weight formula_weight	29852.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	5547

METITVSTPIKQIFPDDAFAETIKANLKKKSVTDAVTQNELNSIDQIIANNSDIKSVQGIQYLPNVRKLMLPRNKLHDISALKELTNLTYLKLHNNQLQSLPNGVFDKLTNLKELSLLFNQLQSLPDGVFDKLTNLTYLNLAHNQLQSLPDGVFDKLTNLTYLNLAHNQLQSLPEGVFDKLTQLKDLRLYQNQLKSVPDGVFDRLTSLQYIWLHDNPWDCTCPGIRNLSEWINKHSGVVRNSAGSVAPDSAKCSGSGKPVRSIICP

来源 Source

来源生物 organism	Cyclostomata
NCBI Class编号 ncbi_taxonomy_id	1476529
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Apoptosis-associated speck-like protein containing a CARD
Molecular weight formula_weight	10220.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

EMGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQ

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	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	154

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8. Citations (1)

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Unit-cell length a length_a	79.481 Å
Unit-cell length b length_b	79.481 Å
Unit-cell length c length_c	279.197 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	16

Space group space_group	P 43 21 2
Space-group number int_tables_number	96
Crystal system crystal_system	tetragonal

Resolution resolution	2.290 Å
Low-resolution limit resolution_low	29.650 Å
R factor r_factor	0.1972
R_work r_work	0.1951
R_free r_free	0.2362

fit	/app/data/saxs_computation/e5/7e5b/7e5b.fit
pddf	/app/data/pr_computation/e5/7e5b/7e5b.pr.out
profile	/app/data/saxs_computation/e5/7e5b/7e5b.dat

Crystal structure of ASC PYD Domain and Rb-B7

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

Apoptosis-associated speck-like protein containing a CARD

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 (4)

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 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)