SAXSdb — 8avo

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

Leptin

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 × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain A； UniProt 22–167 Chain C； UniProt 22–167 Chain E； UniProt 22–167	Not recorded	Leptin receptor × 3 （P48357）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4；20 mM HEPES, 150 mM NaCl, pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 6.84 Å

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 8AVO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AX8 Human obesity protein, leptin Deposited 1997-10-31	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 22–167（146 aa）	Mutation：W100E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；PROTEIN WAS CRYSTALLIZED FROM 1.8M NA FORMATE, 100MM TRIS, PH 7.5	Resolution 2.40 Å R-free 0.283
1AX8 Human obesity protein, leptin Deposited 1997-10-31	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 22–167（146 aa）	Mutation：W100E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；PROTEIN WAS CRYSTALLIZED FROM 1.8M NA FORMATE, 100MM TRIS, PH 7.5	Resolution 2.40 Å R-free 0.283
7Z3Q Crystal structure of the human leptin:LepR-CRH2 encounter complex to 3.6 A resolution. Deposited 2022-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 22–167（146 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；Index screen HT #F1 0.2 M L-proline 0.1 M HEPES pH 7.5 10% PEG 3350 cryo: 25% PEG400	Resolution 3.62 Å R-free 0.305
7Z3Q Crystal structure of the human leptin:LepR-CRH2 encounter complex to 3.6 A resolution. Deposited 2022-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 22–167（146 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；Index screen HT #F1 0.2 M L-proline 0.1 M HEPES pH 7.5 10% PEG 3350 cryo: 25% PEG400	Resolution 3.62 Å R-free 0.305
7Z3Q Crystal structure of the human leptin:LepR-CRH2 encounter complex to 3.6 A resolution. Deposited 2022-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 22–167（146 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；Index screen HT #F1 0.2 M L-proline 0.1 M HEPES pH 7.5 10% PEG 3350 cryo: 25% PEG400	Resolution 3.62 Å R-free 0.305
8AVE Human leptin in complex with the human LEP-R ectodomain fused to a C-terminal trimeric isoleucine GCN4 zipper (2:2 model) Deposited 2022-08-26	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 22–167（146 aa） Chain C 22–167（146 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 5.62 Å
8AVF Human leptin in complex with the human LEP-R ectodomain fused to a C-terminal trimeric isoleucine GCN4 zipper (closed 3:3 model) Deposited 2022-08-26	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 22–167（146 aa） Chain C 22–167（146 aa） Chain E 22–167（146 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.45 Å
8K6Z NMR structure of human leptin Deposited 2023-07-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 22–167（146 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.5；298 K；Ionic strength (raw mmCIF value) 5；Pressure 1 NMR sample composition 0.8 mM [U-13C; U-15N] leptin, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
8X80 Structure of leptin-LepR trimer with a small gap Deposited 2023-11-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain D 1–167（167 aa） Chain E 1–167（167 aa） Chain F 1–167（167 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 15	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.88 Å
8X81 Structure of leptin-LepR trimer with a large gap Deposited 2023-11-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain D 1–167（167 aa） Chain E 1–167（167 aa） Chain F 1–167（167 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 19	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.77 Å
8X85 Structure of leptin-LepR dimer Deposited 2023-11-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–167（167 aa） Chain D 1–167（167 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 11	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.58 Å
9PUO Neutralizing monoclonal antibody Fab fragment bound to leptin Deposited 2025-07-31	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 22–167（146 aa）	Mutation：W100E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；293 K；Protein at 25 mg/ml in 20 mM Hepes pH 7.4 and 75 mM sodium chloride versus a reservoir with 18% PEG 8,000 and 20% glycerol.	Resolution 3.10 Å R-free 0.277
9PUO Neutralizing monoclonal antibody Fab fragment bound to leptin Deposited 2025-07-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 22–167（146 aa）	Mutation：W100E	PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；293 K；Protein at 25 mg/ml in 20 mM Hepes pH 7.4 and 75 mM sodium chloride versus a reservoir with 18% PEG 8,000 and 20% glycerol.	Resolution 3.10 Å R-free 0.277

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

View Construct and Data Evidence

UniProt name	LEP_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 26–171； UniProt 22–167 Author chain C； PDBConstruct 26–171； UniProt 22–167 Author chain E； PDBConstruct 26–171； UniProt 22–167

Leptin receptor

Homo sapiens

UniProt P48357

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 × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain B； UniProt 22–839 Chain D； UniProt 22–839 Chain F； UniProt 22–839	Not recorded	Leptin × 3 （P41159）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4；20 mM HEPES, 150 mM NaCl, pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 6.84 Å

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 8AVO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3V6O Leptin Receptor-antibody complex Deposited 2011-12-20	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 × 3 PDB declaration: trimeric	Chain A 428–633（206 aa） Fragment：Leptin binding domain of human obesity receptor	Not recorded	CYS CYSTEINE × 1 EDO 1,2-ETHANEDIOL × 13 ACT ACETATE ION × 3 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 4.6；281 K；sodium acetate, PEG-4000, pH 4.6, vapor diffusion, temperature 281K	Resolution 1.95 Å R-free 0.213
3V6O Leptin Receptor-antibody complex Deposited 2011-12-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 428–633（206 aa） Fragment：Leptin binding domain of human obesity receptor	Not recorded	CYS CYSTEINE × 1 EDO 1,2-ETHANEDIOL × 18 ACT ACETATE ION × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 4.6；281 K；sodium acetate, PEG-4000, pH 4.6, vapor diffusion, temperature 281K	Resolution 1.95 Å R-free 0.213
6E2P Structure of human JAK2 FERM/SH2 in complex with Leptin Receptor Deposited 2018-07-11	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 × 2 PDB declaration: dimeric	Chain C 863–933（71 aa） Fragment：UNP residues 863-933	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277.15 K；0.1 M MES, pH 6.5, 0.2 M magnesium chloride, 5-10% PEG4000, 10% ethylene glycol	Resolution 2.83 Å R-free 0.243
6E2P Structure of human JAK2 FERM/SH2 in complex with Leptin Receptor Deposited 2018-07-11	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 863–933（71 aa） Fragment：UNP residues 863-933	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277.15 K；0.1 M MES, pH 6.5, 0.2 M magnesium chloride, 5-10% PEG4000, 10% ethylene glycol	Resolution 2.83 Å R-free 0.243
7Z3Q Crystal structure of the human leptin:LepR-CRH2 encounter complex to 3.6 A resolution. Deposited 2022-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 428–635（208 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；Index screen HT #F1 0.2 M L-proline 0.1 M HEPES pH 7.5 10% PEG 3350 cryo: 25% PEG400	Resolution 3.62 Å R-free 0.305
7Z3Q Crystal structure of the human leptin:LepR-CRH2 encounter complex to 3.6 A resolution. Deposited 2022-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 428–635（208 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；Index screen HT #F1 0.2 M L-proline 0.1 M HEPES pH 7.5 10% PEG 3350 cryo: 25% PEG400	Resolution 3.62 Å R-free 0.305
7Z3Q Crystal structure of the human leptin:LepR-CRH2 encounter complex to 3.6 A resolution. Deposited 2022-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 428–635（208 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；Index screen HT #F1 0.2 M L-proline 0.1 M HEPES pH 7.5 10% PEG 3350 cryo: 25% PEG400	Resolution 3.62 Å R-free 0.305
8AVE Human leptin in complex with the human LEP-R ectodomain fused to a C-terminal trimeric isoleucine GCN4 zipper (2:2 model) Deposited 2022-08-26	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 22–839（818 aa） Chain D 22–839（818 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 5.62 Å
8AVF Human leptin in complex with the human LEP-R ectodomain fused to a C-terminal trimeric isoleucine GCN4 zipper (closed 3:3 model) Deposited 2022-08-26	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 22–839（818 aa） Chain D 22–839（818 aa） Chain F 22–839（818 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.45 Å
8X80 Structure of leptin-LepR trimer with a small gap Deposited 2023-11-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 21–839（819 aa） Chain B 21–839（819 aa） Chain C 21–839（819 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 15	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.88 Å
8X81 Structure of leptin-LepR trimer with a large gap Deposited 2023-11-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 21–839（819 aa） Chain B 21–839（819 aa） Chain C 21–839（819 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 19	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.77 Å
8X85 Structure of leptin-LepR dimer Deposited 2023-11-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 21–839（819 aa） Chain B 21–839（819 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 11	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.58 Å

8 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	LEPR_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–818； UniProt 22–839 Author chain D； PDBConstruct 1–818； UniProt 22–839 Author chain F； PDBConstruct 1–818； UniProt 22–839

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	8avo
Deposition date deposition_date	2022-08-26
Structure title title	Human leptin in complex with the human LEP-R ectodomain fused to a C-terminal trimeric isoleucine GCN4 zipper (open 3:3 model).
Keywords keywords	leptin, LEP-R, obesity, metabolism, energy balance, CYTOKINE; CYTOKINE
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	58.20 Å
Radius of gyration Rg (electron density) rg_electron	57.69 Å
Forward intensity I(0) i0	853940000.00
Molecular weight molecular_weight	252840.0 kDa
Excluded volume excluded_volume	319680 Å³
Envelope volume envelope_volume	578370 Å³
Hydration-shell volume shell_volume	83944 Å³
Envelope diameter envelope_diameter	181.3 Å
Shell Rg shell_rg	62.29 Å
Envelope Rg envelope_rg	53.67 Å
Shape Rg shape_rg	57.70 Å
Total Rg total_rg	57.83 Å
Total atoms total_atoms	17811
Residues n_residues	2226
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	175.1 Å
Rg (real space) rg_real	57.75 Å
Rg uncertainty (real space) rg_real_error	1.53 Å
I(0) (real space) i0_real	8.5390e+08
I(0) uncertainty (real space) i0_real_error	1.7220e+07
Rg (reciprocal space) rg_reciprocal	58.57 Å
I(0) (reciprocal space) i0_reciprocal	855000000.0000
Solution quality estimate total_estimate	0.8577
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	84.3 Å
Skewness Skewness skewness	-0.149
Kurtosis Kurtosis kurtosis	-0.478
Angular range angular_range	— – 0.1350 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	32280000.0000
Real-space data points n_real_points	28
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.861; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; Smooth: 0.607

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Leptin
Molecular weight formula_weight	18605.1 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,E
Atom count atom_count	17811

AHHHHHHPGGPGSENLYFQGGSTGGVPIQKVQDDTKTLIKTIVTRINDISHTQSVSSKQKVTGLDFIPGLHPILTLSKMDQTLAVYQQILTSMPSRNVIQISNDLENLRDLLHVLAFSKSCHLPWASGLETLDSLGGVLEASGYSTEVVALSRLQGSLQDMLWQLDLSPGC

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	Homo sapiens

Entity 2 Entity 2 polymer

Description description	Leptin receptor
Molecular weight formula_weight	98822.1 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

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

FNLSYPITPWRFKLSCMPPNSTYDYFLLPAGLSKNTSNSNGHYETAVEPKFNSSGTHFSNLSKTTFHCCFRSEQDRNCSLCADNIEGKTFVSTVNSLVFQQIDANWNIQCWLKGDLKLFICYVESLFKNLFRNYNYKVHLLYVLPEVLEDSPLVPQKGSFQMVHCNCSVHECCECLVPVPTAKLNDTLLMCLKITSGGVIFQSPLMSVQPINMVKPDPPLGLHMEITDDGNLKISWSSPPLVPFPLQYQVKYSENSTTVIREADKIVSATSLLVDSILPGSSYEVQVRGKRLDGPGIWSDWSTPRVFTTQDVIYFPPKILTSVGSNVSFHCIYKKENKIVPSKEIVWWMNLAEKIPQSQYDVVSDHVSKVTFFNLNETKPRGKFTYDAVYCCNEHECHHRYAELYVIDVNINISCETDGYLTKMTCRWSTSTIQSLAESTLQLRYHRSSLYCSDIPSIHPISEPKDCYLQSDGFYECIFQPIFLLSGYTMWIRINHSLGSLDSPPTCVLPDSVVKPLPPSSVKAEITINIGLLKISWEKPVFPENNLQFQIRYGLSGKEVQWKMYEVYDAKSKSVSLPVPDLCAVYAVQVRCKRLDGLGYWSNWSNPAYTVVMDIKVPMRGPEFWRIINGDTMKKEKNVTLLWKPLMKNDSLCSVQRYVINHHTSCNGTWSEDVGNHTKFTFLWTEQAHTVTVLAINSIGASVANFNLTFSWPMSKVNIVQSLSAYPLNSSCVIVSWILSPSDYKLMYFIIEWKNLNEDGEIKWLRISSSVKKYYIHDHFIPIEKYQFSLYPIFMEGVGKPKIINSFTQDDIEKHQSDSTGGSGGSGGSGGSGGSRMKQIEDKIEEILSKIYHIENEIARIKKLIGER

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	Homo sapiens

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	triclinic

Resolution resolution	6.84 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	30353

fit	/app/data/saxs_computation/av/8avo/8avo.fit
pddf	/app/data/pr_computation/av/8avo/8avo.pr.out
profile	/app/data/saxs_computation/av/8avo/8avo.dat

Human leptin in complex with the human LEP-R ectodomain fused to a C-terminal trimeric isoleucine GCN4 zipper (open 3:3 model).

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

Leptin

State in the Current Structure

Other States of the Same Protein in the Database

Leptin receptor

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)