SAXSdb — 6zvo

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

Mixed lineage kinase domain-like protein

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 2–150	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；277 K；31 % Polyethylene glycol monomethyl ether 2,000, 0.15 M Potassium bromide, 0.1 M TRIS, pH 9	Resolution 1.37 Å R-free 0.234
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain B； UniProt 2–150	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；277 K；31 % Polyethylene glycol monomethyl ether 2,000, 0.15 M Potassium bromide, 0.1 M TRIS, pH 9	Resolution 1.37 Å R-free 0.234
3	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain C； UniProt 2–150	Not recorded	CL CHLORIDE ION × 1 BR BROMIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；277 K；31 % Polyethylene glycol monomethyl ether 2,000, 0.15 M Potassium bromide, 0.1 M TRIS, pH 9	Resolution 1.37 Å R-free 0.234

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 6ZVO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2MSV Solution structure of the MLKL N-terminal domain Deposited 2014-08-07	Different construct Different mutation/modification 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 1–154（154 aa） Fragment：N-terminal domain, residues 1-154	Mutation：M1L	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0.12；Pressure ambient NMR sample composition 1.5 mM [U-99% 13C; U-99% 15N] protein, 20 mM HEPES, 100 mM sodium chloride, 2 mM TCEP, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 1.5 mM [U-99% 15N] protein, 20 mM HEPES, 100 mM sodium chloride, 2 mM TCEP, 100% D2O \| 100% D2O	Resolution not provided
4M67 Crystal structure of the human MLKL kinase-like domain Deposited 2013-08-09	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 179–471（293 aa） Fragment：UNP residues 179-471	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；0.1M MES, 13% PEG 6000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.90 Å R-free 0.225
4MWI Crystal structure of the human MLKL pseudokinase domain Deposited 2013-09-25	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 183–471（289 aa） Fragment：unp residues 183-471	Not recorded	PXN (2S)-1-[3-{[(2R)-2-hydroxypropyl]oxy}-2,2-bis({[(2R)-2-hydroxypropyl]oxy}methyl)propoxy]propan-2-ol × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；25% w/v pentaerythitol propoxylate, 0.1M Tris chloride, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.70 Å R-free 0.194
5KNJ Pseudokinase Domain of MLKL bound to Compound 1. Deposited 2016-06-28	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 191–471（281 aa） Fragment：UNP residues 191-471	Not recorded	6UX 1-[4-[methyl-[2-[(3-sulfamoylphenyl)amino]pyrimidin-4-yl]amino]phenyl]-3-[4-(trifluoromethyloxy)phenyl]urea × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；0.1M Na Citrate and 15% PEG3350	Resolution 2.88 Å R-free 0.256
5KNJ Pseudokinase Domain of MLKL bound to Compound 1. Deposited 2016-06-28	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 191–471（281 aa） Fragment：UNP residues 191-471	Not recorded	6UX 1-[4-[methyl-[2-[(3-sulfamoylphenyl)amino]pyrimidin-4-yl]amino]phenyl]-3-[4-(trifluoromethyloxy)phenyl]urea × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；0.1M Na Citrate and 15% PEG3350	Resolution 2.88 Å R-free 0.256
5KO1 Pseudokinase Domain of MLKL bound to Compound 4. Deposited 2016-06-29	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 191–471（281 aa） Fragment：UNP residues 191-471	Not recorded	6UY [(1~{R})-2-[(4-fluorophenyl)amino]-2-oxidanylidene-1-phenyl-ethyl] 3-azanylpyrazine-2-carboxylate × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；0.1M BisTRIS pH 6.5 20% PEG3350	Resolution 2.16 Å R-free 0.226
6BWK Crystal structure of the human MLKL pseudokinase domain T357E/S358E mutant Deposited 2017-12-15	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 190–471（282 aa） Fragment：UNP Residues 190-471	Mutation：T357E S358E	GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；5% w/v polyethylene glycol 8000, 20% v/v polyethylene glycol 300, 0.1M Tris chloride pH 8.5, 10% v/v glycerol	Resolution 2.79 Å R-free 0.297
6D74 Direct Activation of the Executioner Domain of MLKL by a Select Repertoire of Inositol Phosphates Deposited 2018-04-24	Different construct 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 1–156（156 aa） Fragment：residues 1-156	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；303 K；Ionic strength (raw mmCIF value) 0；Pressure 1 NMR sample composition 500 uM [U-13C; U-15N] protein, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
6LK5 MLKL mutant - T357ES358D Deposited 2019-12-18	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 1–471（471 aa）	Mutation：T357E, S358D	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；5%(v/v) 2-Methyl-2,4-pentanediol, 0.1M HEPES(pH7.5), 10%(w/v) PEG 10000	Resolution 2.50 Å R-free 0.238
6LK6 MLKL mutant - T357AS358A Deposited 2019-12-18	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 179–471（293 aa）	Mutation：T357A, S358A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；14%(w/v) PEG 6000, 5% EG, 0.1M HEPES(pH7.5)	Resolution 2.41 Å R-free 0.247
6O5Z Crystal Structure of the human MLKL pseudokinase domain bound to compound 2 Deposited 2019-03-04	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 190–471（282 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.88；293 K；0.18 M magnesium chloride, 26.8% (w/v) PEG 3350, 0.1 M sodium HEPES pH 7.88	Resolution 2.29 Å R-free 0.232
6O5Z Crystal Structure of the human MLKL pseudokinase domain bound to compound 2 Deposited 2019-03-04	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 190–471（282 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 1 LN4 1-[2-fluoranyl-5-(trifluoromethyl)phenyl]-3-[4-[methyl-[2-[(3-sulfamoylphenyl)amino]pyrimidin-4-yl]amino]phenyl]urea × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.88；293 K；0.18 M magnesium chloride, 26.8% (w/v) PEG 3350, 0.1 M sodium HEPES pH 7.88	Resolution 2.29 Å R-free 0.232
6UX8 Structure of monobody 33 MLKL N-terminal domain complex Deposited 2019-11-07	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 5–154（150 aa）	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；25% PEG-MME 550, 0.1 M MES pH 6.5, 0.01 M Zinc acetate	Resolution 2.50 Å R-free 0.296
6ZLE Solution structure of unliganded MLKL executioner domain Deposited 2020-06-30	Different construct 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 2–154（153 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.5；298 K；Ionic strength (raw mmCIF value) 20 mM sodium phosphate,150 mM sodium chloride；Pressure 1 NMR measurement conditions pH 7.1；298 K；Ionic strength (raw mmCIF value) 20 mM sodium phosphate,150 mM sodium chloride；Pressure 1 NMR sample composition 400 uM [U-13C; U-15N] MLKL, 93% H2O/7% D2O \| 93% H2O/7% D2O NMR sample composition 430 uM [U-13C; U-15N] MLKL, 100% D2O \| 100% D2O	Resolution not provided
6ZPR Solution structure of MLKL executioner domain in complex with a covalent inhibitor Deposited 2020-07-09	Different construct Different mutation/modification 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 2–85（84 aa） Chain A 86–154（69 aa）	Not recorded	QOK 7-(2-methoxyethoxymethyl)-1,3-dimethyl-purine-2,6-dione × 1	SOLUTION NMR NMR measurement conditions pH 7.5；298 K；Ionic strength (raw mmCIF value) 20 mM sodium phosphate, 150 mM sodium chloride；Pressure 1 NMR measurement conditions pH 7.1；298 K；Ionic strength (raw mmCIF value) 20 mM sodium phosphate, 150 mM sodium chloride；Pressure 1 NMR sample composition 340 uM [U-13C; U-15N] MLKL, 1200 uM Compound, 93% H2O/7% D2O \| 93% H2O/7% D2O NMR sample composition 385 uM [U-13C; U-15N] MLKL, 840 uM Compound, 100% D2O \| 100% D2O	Resolution not provided
6ZZ1 Crystal structure of MLKL executioner domain in complex with a covalent inhibitor Deposited 2020-08-03	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–150（149 aa）	Not recorded	QOK 7-(2-methoxyethoxymethyl)-1,3-dimethyl-purine-2,6-dione × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；32 % Polyethylene glycol monomethyl ether 2,000, 0.15 M Potassium bromide, 0.1 M TRIS, pH 9	Resolution 1.64 Å R-free 0.231
6ZZ1 Crystal structure of MLKL executioner domain in complex with a covalent inhibitor Deposited 2020-08-03	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–150（149 aa）	Not recorded	QOK 7-(2-methoxyethoxymethyl)-1,3-dimethyl-purine-2,6-dione × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；32 % Polyethylene glycol monomethyl ether 2,000, 0.15 M Potassium bromide, 0.1 M TRIS, pH 9	Resolution 1.64 Å R-free 0.231
7JW7 Structure of monobody 27 human MLKL pseudokinase domain complex Deposited 2020-08-25	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 190–471（282 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；281.15 K；0.2 M magnesium chloride, 20% w/v PEG 3350	Resolution 2.63 Å R-free 0.281
7JXU Structure of monobody 32 human MLKL pseudokinase domain complex Deposited 2020-08-28	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 190–471（282 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；281.15 K；0.1 M Bis-Tris chloride, pH 6.5, 20 % w/v PEG monomethyl ether 5000	Resolution 2.44 Å R-free 0.240
7JXU Structure of monobody 32 human MLKL pseudokinase domain complex Deposited 2020-08-28	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 190–471（282 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；281.15 K；0.1 M Bis-Tris chloride, pH 6.5, 20 % w/v PEG monomethyl ether 5000	Resolution 2.44 Å R-free 0.240
7MON Structure of human RIPK3-MLKL complex Deposited 2021-05-03	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 190–471（282 aa）	Not recorded	ZL1 N-[4-({2-[(cyclopropanecarbonyl)amino]pyridin-4-yl}oxy)-3-fluorophenyl]-1-(4-fluorophenyl)-2-oxo-1,2-dihydropyridine-3-carboxamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；281.15 K；0.2 M ammonium acetate 30%w/v PEG 4000 0.1 M trisodium citrate-citric acid pH 5.5	Resolution 2.23 Å R-free 0.260
7NM2 Solution structure of MLKL executioner domain in complex with a fragment Deposited 2021-02-23	Different construct 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 2–154（153 aa）	Not recorded	UJ5 2-[(~{S})-methoxy-(4-propan-2-ylphenyl)methyl]-3~{H}-benzimidazole-5-carboxylic acid × 1	SOLUTION NMR NMR measurement conditions pH 7.1；298 K；Ionic strength (raw mmCIF value) 170；Pressure 1 NMR measurement conditions pH 7.5；298 K；Ionic strength (raw mmCIF value) 170；Pressure 1 NMR sample composition 430 uM [U-13C; U-15N] MLKL executioner domain, 700 uM Cpd 5, 100% D2O \| 100% D2O NMR sample composition 400 uM [U-13C; U-15N] MLKL executioner domain, 700 uM Cpd 5, 93% H2O/7% D2O \| 93% H2O/7% D2O	Resolution not provided
7NM4 Solution structure of MLKL executioner domain in complex with a fragment Deposited 2021-02-23	Different construct 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 2–154（153 aa）	Not recorded	UJ8 (~{S})-1~{H}-benzimidazol-2-yl-(4-propan-2-ylphenyl)methanol × 1	SOLUTION NMR NMR measurement conditions pH 7.1；298 K；Ionic strength (raw mmCIF value) 170；Pressure 1 NMR measurement conditions pH 7.5；298 K；Ionic strength (raw mmCIF value) 170；Pressure 1 NMR sample composition 385 uM [U-13C; U-15N] MLKL executioner domain, 2000 uM Cpd 3, 100% D2O \| 100% D2O NMR sample composition 315 uM [U-13C; U-15N] MLKL executioner domain, 1600 uM Cpd 3, 93% H2O/7% D2O \| 93% H2O/7% D2O	Resolution not provided
7NM5 Solution structure of MLKL executioner domain in complex with a fragment Deposited 2021-02-23	Different construct 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 2–154（153 aa）	Not recorded	UJ2 2-[(~{S})-methoxy-(4-phenylphenyl)methyl]-3~{H}-benzimidazole-5-carboxylic acid × 1	SOLUTION NMR NMR measurement conditions pH 7.5；298 K；Ionic strength (raw mmCIF value) 170；Pressure 1 NMR measurement conditions pH 7.1；298 K；Ionic strength (raw mmCIF value) 170；Pressure 1 NMR sample composition 400 uM [U-13C; U-15N] MLKL executioner domain, 700 uM Cpd 7, 93% H2O/7% D2O \| 93% H2O/7% D2O NMR sample composition 430 uM [U-13C; U-15N] MLKL executioner domain, 700 uM Cpd 7, 100% D2O \| 100% D2O	Resolution not provided
8SLZ Crystal structure of phosphorylated (T357/S358) human MLKL pseudokinase domain Deposited 2023-04-25	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 190–471（282 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；0.1 M HEPES pH 7.5, 20%w/v PEG 8000	Resolution 2.30 Å R-free 0.234

21 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MLKL_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–153； UniProt 2–150 Author chain B； PDBConstruct 5–153； UniProt 2–150 Author chain C； PDBConstruct 5–153； UniProt 2–150

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	6zvo
Deposition date deposition_date	2020-07-27
Structure title title	Crystal structure of unliganded MLKL executioner domain
Keywords keywords	Necroptosis, LIPID BINDING PROTEIN; LIPID BINDING PROTEIN
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	27.25 Å
Radius of gyration Rg (electron density) rg_electron	26.58 Å
Forward intensity I(0) i0	44780300.00
Molecular weight molecular_weight	49928.0 kDa
Excluded volume excluded_volume	61965 Å³
Envelope volume envelope_volume	81362 Å³
Hydration-shell volume shell_volume	26765 Å³
Envelope diameter envelope_diameter	93.1 Å
Shell Rg shell_rg	32.61 Å
Envelope Rg envelope_rg	26.30 Å
Shape Rg shape_rg	26.57 Å
Total Rg total_rg	27.31 Å
Total atoms total_atoms	3486
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	87.9 Å
Rg (real space) rg_real	27.30 Å
Rg uncertainty (real space) rg_real_error	0.54 Å
I(0) (real space) i0_real	4.4780e+07
I(0) uncertainty (real space) i0_real_error	5.9070e+05
Rg (reciprocal space) rg_reciprocal	27.29 Å
I(0) (reciprocal space) i0_reciprocal	44780000.0000
Solution quality estimate total_estimate	0.9018
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	31.8 Å
Skewness Skewness skewness	0.341
Kurtosis Kurtosis kurtosis	-0.470
Angular range angular_range	— – 0.2900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	13860000.0000
Real-space data points n_real_points	59
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.983

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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	Mixed lineage kinase domain-like protein
Molecular weight formula_weight	17642.3 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	4148

GSPGENLKHIITLGQVIHKRCEEMKYCKKQCRRLGHRVLGLIKPLEMLQDQGKRSVPSEKLTTAMNRFKAALEEANGEIEKFSNRSNICRFLTASQDKILFKDVNRKLSDVWKELSLLLQVEQRMPVSPISQGASWAQEDQQDADEDRRAFQM

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 2 Entity 2 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 3 Entity 3 non-polymer

Description description	BROMIDE ION
Molecular weight formula_weight	79.9 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	450

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8. Citations (1)

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Unit-cell length a length_a	56.057 Å
Unit-cell length b length_b	53.501 Å
Unit-cell length c length_c	70.912 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	98.36 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	6

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

Resolution resolution	1.371 Å
Low-resolution limit resolution_low	70.160 Å
R factor r_factor	0.1918
R_work r_work	0.1896
R_free r_free	0.2335

fit	/app/data/saxs_computation/zv/6zvo/6zvo.fit
pddf	/app/data/pr_computation/zv/6zvo/6zvo.pr.out
profile	/app/data/saxs_computation/zv/6zvo/6zvo.dat

Crystal structure of unliganded MLKL executioner domain

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

Mixed lineage kinase domain-like protein

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