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5knj

Pseudokinase Domain of MLKL bound to Compound 1.

Method: X-RAY DIFFRACTION Dmax: 87.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Mixed lineage kinase domain-like protein

Homo sapiens

UniProt Q8NB16

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 191–471 Fragment：UNP residues 191-471 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
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 191–471 Fragment：UNP residues 191-471 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

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 5KNJ 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
5KO1 Pseudokinase Domain of MLKL bound to Compound 4. Deposited 2016-06-29 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
6ZVO Crystal structure of unliganded MLKL executioner domain Deposited 2020-07-27 Different construct 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 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
6ZVO Crystal structure of unliganded MLKL executioner domain Deposited 2020-07-27 Different construct 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 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
6ZVO Crystal structure of unliganded MLKL executioner domain Deposited 2020-07-27 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 2–150（149 aa）
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
6ZZ1 Crystal structure of MLKL executioner domain in complex with a covalent inhibitor Deposited 2020-08-03 Different construct 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 construct 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 26 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 3–283； UniProt 191–471 Author chain B； PDBConstruct 3–283； UniProt 191–471

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

SAXS profile for 5knj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5knj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5knj
Deposition date deposition_date2016-06-28
Structure title titlePseudokinase Domain of MLKL bound to Compound 1.
Keywords keywordsPseudokinase domain MLKL Compound 1 GFE Out Type 2 inhibitor, MEMBRANE PROTEINS-INHIBITOR complex; MEMBRANE PROTEINS/INHIBITOR
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier26.13 Å
Radius of gyration Rg (electron density) rg_electron25.17 Å
Forward intensity I(0) i052716200.00
Molecular weight molecular_weight57910.0 kDa
Excluded volume excluded_volume73110 ų
Envelope volume envelope_volume87444 ų
Hydration-shell volume shell_volume29275 ų
Envelope diameter envelope_diameter90.2 Å
Shell Rg shell_rg32.30 Å
Envelope Rg envelope_rg25.44 Å
Shape Rg shape_rg25.18 Å
Total Rg total_rg25.92 Å
Total atoms total_atoms4080
Residues n_residues511
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax87.6 Å
Rg (real space) rg_real26.14 Å
Rg uncertainty (real space) rg_real_error0.58 Å
I(0) (real space) i0_real5.2720e+07
I(0) uncertainty (real space) i0_real_error6.9810e+05
Rg (reciprocal space) rg_reciprocal26.14 Å
I(0) (reciprocal space) i0_reciprocal52720000.0000
Solution quality estimate total_estimate0.8791
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary86.1 Å
Skewness Skewness skewness0.387
Kurtosis Kurtosis kurtosis-0.223
Angular range angular_range— – 0.3050 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12550000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.845; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.905
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5knja_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.0 — automated matches
Domain ID domain_idd5knjb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.0 — automated matches

CATH v4.4 (4 domains)

Domain ID domain_id5knjA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id5knjA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
Domain ID domain_id5knjB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id5knjB02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
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8. Citations (1)

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9. Files and Curves (10)