SAXSdb — 8s93

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

Tyrosine-protein kinase BTK

Mus musculus

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 1–171 Chain A； UniProt 396–659	Fragment：PHTH domain residues 1-171 and Kinase domain residues 396-659 Mutation：Q91A, I92A, I94A, I95A, K430R, L542M S543T, V555T, R562K, S564A, P565S, Y617P	9AJ 2-[3'-(hydroxymethyl)-1-methyl-5-({5-[(2S)-2-methyl-4-(oxetan-3-yl)piperazin-1-yl]pyridin-2-yl}amino)-6-oxo[1,6-dihydro[3,4'-bipyridine]]-2'-yl]-7,7-dimethyl-3,4,7,8-tetrahydro-2H-cyclopenta[4,5]pyrrolo[1,2-a]pyrazin-1(6H)-one × 1 ZN ZINC ION × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 5.6；277 K；20%PEG3350, 0.1M Bis-Tris, pH5.6, 0.2M magnesium chloride	Resolution 2.10 Å R-free 0.246

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 8S93	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4XI2 Crystal Structure of an auto-inhibited form of Bruton's Tryrosine Kinase Deposited 2015-01-06	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 214–659（446 aa） Fragment：UNP residues 214-659	Not recorded	AU GOLD ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；Mix purified dimer protein at 5 mg/ml in 25 mM TRIS.Cl, pH 8.5, 10 mM NaCl, 5 mM DTT with an equal volume of the precipitant solution, 100 mM TRIS.Cl, pH 8.5, 200 mM Na.acetate, 7.5 % PEG 4,000, then suspend over 1 ml of precipitant solution. Wedge shaped crystals grew to approximately 0.1 mm on a side after a period of two weeks. Crystals were frozen by first transferring them, in four sequential steps, to a solution of 100 mM TRIS.Cl, pH 8.5, 200 mM Na.acetate, 15 % PEG 4,000. This was followed by transfer in six sequential steps to a solution containing 100 mM TRIS.Cl, pH 8.5, 200 mM Na.acetate, 15 % PEG 4,000, 30% glucose	Resolution 2.60 Å R-free 0.248
8FD9 Structure of BTK kinase domain with the second-generation inhibitor acalabrutinib Deposited 2022-12-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 396–659（264 aa）	Mutation：K430R, L542M S543T, V555T, R562K, S564A, P565S, Y617P	XQQ 4-[(4S)-8-amino-3-{(2S)-1-[(2E)-but-2-enoyl]pyrrolidin-2-yl}imidazo[1,5-a]pyrazin-1-yl]-N-(pyridin-2-yl)benzamide × 1 BR BROMIDE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6.5；277 K；20% PEG 3350, 0.1M Bis-tris propane, pH 6.5 and 0.2M sodium bromide	Resolution 1.70 Å R-free 0.228
8FF0 Structure of BTK kinase domain with the second-generation inhibitor tirabrutinib Deposited 2022-12-07	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 396–659（264 aa）	Mutation：K430R, L542M S543T, V555T, R562K, S564A, P565S, Y617P	7GB 6-azanyl-9-[(3~{R})-1-[(~{E})-but-2-enoyl]pyrrolidin-3-yl]-7-(4-phenoxyphenyl)purin-8-one × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；16% PEG 8000 and 0.1M sodium citrate	Resolution 2.60 Å R-free 0.267
8GMB Crystal structure of the full-length Bruton's tyrosine kinase (PH-TH domain not visible) Deposited 2023-03-24	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 1–659（659 aa）	Mutation：E298A, K300A, E301A, A384P, S386P, T387P, A388P, L390F, K430R, L542M S543T, V555T, R562K, S564A, P565S, Y617P	9AJ 2-[3'-(hydroxymethyl)-1-methyl-5-({5-[(2S)-2-methyl-4-(oxetan-3-yl)piperazin-1-yl]pyridin-2-yl}amino)-6-oxo[1,6-dihydro[3,4'-bipyridine]]-2'-yl]-7,7-dimethyl-3,4,7,8-tetrahydro-2H-cyclopenta[4,5]pyrrolo[1,2-a]pyrazin-1(6H)-one × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；277.15 K；20% PEG 3350, 0.1M Bis-Tris Propane, 0.2M potassium thiocyanate	Resolution 3.40 Å R-free 0.289
8S9F Crystal structure of the kinase domain of Bruton's Tyrosine Kinase bound to dasatinib Deposited 2023-03-28	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 382–659（278 aa） Chain B 382–659（278 aa）	Mutation：L390G, Y551E, Y617P Mutation：L390G, Y551E, Y617P	1N1 N-(2-CHLORO-6-METHYLPHENYL)-2-({6-[4-(2-HYDROXYETHYL)PIPERAZIN-1-YL]-2-METHYLPYRIMIDIN-4-YL}AMINO)-1,3-THIAZOLE-5-CARBOXAMIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；42% PEG200, 0.1M HEPES	Resolution 2.60 Å R-free 0.284
9EJJ Bruton's tyrosine kinase in complex with compound PTI55 Deposited 2024-11-28	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 382–659（278 aa）	Mutation：L390G, Y551E, Y617P	A1BIZ 4-{4-amino-1-[(3R)-1-(cyclopropanecarbonyl)piperidin-3-yl]-1H-pyrazolo[3,4-d]pyrimidin-3-yl}-N-[4-(trifluoromethoxy)pyridin-2-yl]benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1M NaCitrate pH 5.5, 18% PEG3350	Resolution 2.03 Å R-free 0.242
9EJJ Bruton's tyrosine kinase in complex with compound PTI55 Deposited 2024-11-28	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 382–659（278 aa）	Mutation：L390G, Y551E, Y617P	A1BIZ 4-{4-amino-1-[(3R)-1-(cyclopropanecarbonyl)piperidin-3-yl]-1H-pyrazolo[3,4-d]pyrimidin-3-yl}-N-[4-(trifluoromethoxy)pyridin-2-yl]benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1M NaCitrate pH 5.5, 18% PEG3350	Resolution 2.03 Å R-free 0.242
9EJR Bruton's tyrosine kinase in complex with compound PTI52 Deposited 2024-11-28	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 382–659（278 aa）	Mutation：L390G, Y551E, Y617P	A1BI0 4-{4-amino-1-[(3R)-1-(cyclopropanecarbonyl)piperidin-3-yl]-1H-pyrazolo[3,4-d]pyrimidin-3-yl}-N-(4-cyclopropylpyridin-2-yl)benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1M NaCitrate pH 5.5, 18% PEG3350	Resolution 2.10 Å R-free 0.295
9EJR Bruton's tyrosine kinase in complex with compound PTI52 Deposited 2024-11-28	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 382–659（278 aa）	Mutation：L390G, Y551E, Y617P	A1BI0 4-{4-amino-1-[(3R)-1-(cyclopropanecarbonyl)piperidin-3-yl]-1H-pyrazolo[3,4-d]pyrimidin-3-yl}-N-(4-cyclopropylpyridin-2-yl)benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1M NaCitrate pH 5.5, 18% PEG3350	Resolution 2.10 Å R-free 0.295
9EJS Bruton's tyrosine kinase with mutations in the activation loop in complex with compound PTI52 Deposited 2024-11-28	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 396–659（264 aa）	Mutation：K430R, L542M, S543T, V555T, R562K, S564A, P565S	A1BI0 4-{4-amino-1-[(3R)-1-(cyclopropanecarbonyl)piperidin-3-yl]-1H-pyrazolo[3,4-d]pyrimidin-3-yl}-N-(4-cyclopropylpyridin-2-yl)benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；Sodium citrate tribasic dihydrate pH 5.5, 16% w/v Polyethylene glycol 8,000	Resolution 2.26 Å R-free 0.246
9EJS Bruton's tyrosine kinase with mutations in the activation loop in complex with compound PTI52 Deposited 2024-11-28	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 396–659（264 aa）	Mutation：K430R, L542M, S543T, V555T, R562K, S564A, P565S	A1BI0 4-{4-amino-1-[(3R)-1-(cyclopropanecarbonyl)piperidin-3-yl]-1H-pyrazolo[3,4-d]pyrimidin-3-yl}-N-(4-cyclopropylpyridin-2-yl)benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；Sodium citrate tribasic dihydrate pH 5.5, 16% w/v Polyethylene glycol 8,000	Resolution 2.26 Å R-free 0.246
9EJS Bruton's tyrosine kinase with mutations in the activation loop in complex with compound PTI52 Deposited 2024-11-28	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 396–659（264 aa）	Mutation：K430R, L542M, S543T, V555T, R562K, S564A, P565S	A1BI0 4-{4-amino-1-[(3R)-1-(cyclopropanecarbonyl)piperidin-3-yl]-1H-pyrazolo[3,4-d]pyrimidin-3-yl}-N-(4-cyclopropylpyridin-2-yl)benzamide × 1 DMS DIMETHYL SULFOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；Sodium citrate tribasic dihydrate pH 5.5, 16% w/v Polyethylene glycol 8,000	Resolution 2.26 Å R-free 0.246
9EJX Bruton's tyrosine kinase with mutations in the activation loop in complex with compound PTI42 Deposited 2024-11-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 396–659（264 aa）	Mutation：K430R, L542M, S543T, V555T, R562K, S564A, P565S,Y617P	A1BI1 {(3R)-3-[4-amino-3-(4-phenoxyphenyl)-1H-pyrazolo[3,4-d]pyrimidin-1-yl]piperidin-1-yl}(cyclopropyl)methanone × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1 M Sodium citrate tribasic dihydrate pH 5.5, 18% w/v Polyethylene glycol 8,000	Resolution 2.86 Å R-free 0.296
9ME2 Bruton's tyrosine kinase with mutations in the activation loop in complex with compound A110162 Deposited 2024-12-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 396–659（264 aa）	Mutation：K430R, L542M, S543T, V555T, R562K, S564A, P565S,Y617P	A1BKW 3-(4-phenoxyphenyl)-1-[(3S)-piperidin-3-yl]-1H-pyrazolo[3,4-d]pyrimidin-4-amine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1 M Sodium citrate tribasic dihydrate pH 5.5, 18% w/v Polyethylene glycol 8,000	Resolution 3.38 Å R-free 0.286
9ME3 Bruton's tyrosine kinase with mutations in the activation loop in complex with compound P301390 Deposited 2024-12-06	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 396–659（264 aa）	Mutation：K430R, L542M, S543T, V555T, R562K, S564A, P565S,Y617P	A1BJE 3-(4-phenoxyphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1 M Sodium citrate tribasic dihydrate pH 5.5, 18% w/v Polyethylene glycol 8,000	Resolution 3.05 Å R-free 0.288
9ZLJ Crystal structure of BTK kinase domain bound to compound YS1 Deposited 2025-12-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 382–659（278 aa）	Mutation：Y617P	A1C20 N-{(1r,4r)-4-[2-(4-chlorophenoxy)acetamido]cyclohexyl}-N-[2-(4-methyl-1H-pyrrolo[2,3-b]pyridin-3-yl)ethyl]propanamide × 1 IMD IMIDAZOLE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277 K；15-25% PEG3350, 0.1M imidazole	Resolution 1.60 Å R-free 0.218
9ZLM Crystal structure of BTK kinase domain bound to compound YS2 Deposited 2025-12-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 382–659（278 aa）	Mutation：Y617P	A1C2Z N-[4-(3-{2-oxo-2-[3-(phenoxymethyl)azetidin-1-yl]acetamido}phenyl)oxan-4-yl]propanamide × 1 IMD IMIDAZOLE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277 K；15-25% PEG3350, 0.1M imidazole	Resolution 1.27 Å R-free 0.212

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

View Construct and Data Evidence

UniProt name	BTK_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–171； UniProt 1–171 Author chain A； PDBConstruct 194–457； UniProt 396–659

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	8s93
Deposition date deposition_date	2023-03-27
Structure title title	Crystal structure of the PH-TH/kinase complex of Bruton's tyrosine kinase
Keywords keywords	;Bruton's tyrosine kinase, Non-receptor tyrosine kinase, complex, lipid-binding, ATP-binding, TRANSFERASE ;; TRANSFERASE
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	26.76 Å
Radius of gyration Rg (electron density) rg_electron	26.08 Å
Forward intensity I(0) i0	41126300.00
Molecular weight molecular_weight	50169.0 kDa
Excluded volume excluded_volume	62969 Å³
Envelope volume envelope_volume	77300 Å³
Hydration-shell volume shell_volume	25579 Å³
Envelope diameter envelope_diameter	95.1 Å
Shell Rg shell_rg	32.42 Å
Envelope Rg envelope_rg	26.54 Å
Shape Rg shape_rg	26.11 Å
Total Rg total_rg	26.71 Å
Total atoms total_atoms	6973
Residues n_residues	429
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	93.0 Å
Rg (real space) rg_real	26.92 Å
Rg uncertainty (real space) rg_real_error	0.84 Å
I(0) (real space) i0_real	4.1130e+07
I(0) uncertainty (real space) i0_real_error	5.9840e+05
Rg (reciprocal space) rg_reciprocal	26.88 Å
I(0) (reciprocal space) i0_reciprocal	41120000.0000
Solution quality estimate total_estimate	0.8431
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	26.8 Å
Skewness Skewness skewness	0.501
Kurtosis Kurtosis kurtosis	-0.267
Angular range angular_range	— – 0.2950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	12520000.0000
Real-space data points n_real_points	60
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.752; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.770; Smooth: 0.931

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Tyrosine-protein kinase BTK
Molecular weight formula_weight	52320.7 kDa
EC 编号 ec_number	2.7.10.2
Mutation mutation	Q91A, I92A, I94A, I95A, K430R, L542M S543T, V555T, R562K, S564A, P565S, Y617P
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	7273

MAAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYEYDFERGRRGSKKGSIDVEKITCVETVIPEKNPPPERQIPRRGEESSEMEAASAAERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILENRGGGSGGGGSGGGGSGGGGSGGGEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIRMIREGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGMTRYVLDDEYTSSTGSKFPVKWASPEVLMYSKFSSKSDIWAFGVLMWEIYSLGKMPYERFTNSETAEHIAQGLRLPRPHLASERVYTIMYSCWHEKADERPSFKILLSNILDVMDEES

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	house mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	;2-[3'-(hydroxymethyl)-1-methyl-5-({5-[(2S)-2-methyl-4-(oxetan-3-yl)piperazin-1-yl]pyridin-2-yl}amino)-6-oxo[1,6-dihydro[3,4'-bipyridine]]-2'-yl]-7,7-dimethyl-3,4,7,8-tetrahydro-2H-cyclopenta[4,5]pyrrolo[1,2-a]pyrazin-1(6H)-one ;
Molecular weight formula_weight	664.8 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	178

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7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id	8s93A01
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	29 — PH-domain like
Homologous superfamily homologous superfamily	30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Domain ID domain_id	8s93A02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily	20 — Phosphorylase Kinase; domain 1

Domain ID domain_id	8s93A03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily	10 — Transferase(Phosphotransferase) domain 1

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8. Citations (1)

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Unit-cell length a length_a	38.376 Å
Unit-cell length b length_b	77.383 Å
Unit-cell length c length_c	82.323 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	97.98 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	2

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	monoclinic

Resolution resolution	2.100 Å
Low-resolution limit resolution_low	19.710 Å
R factor r_factor	0.2006
R_work r_work	0.1982
R_free r_free	0.2465

fit	/app/data/saxs_computation/s9/8s93/8s93.fit
pddf	/app/data/pr_computation/s9/8s93/8s93.pr.out
profile	/app/data/saxs_computation/s9/8s93/8s93.dat

Crystal structure of the PH-TH/kinase complex of Bruton's tyrosine kinase

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

Tyrosine-protein kinase BTK

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