SAXSdb — 8vjx

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

Neurolysin, mitochondrial

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 38–704	Not recorded	Bradykinin × 1 （P01042） ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；17.5 ~ 30 % polyethylene glycol 3,350 and 50 ~ 125 mM Bis-Tris HCl buffer, pH 6.5	Resolution 2.89 Å R-free 0.255

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 8VJX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5LUZ Structure of Human Neurolysin (E475Q) in complex with neurotensin peptide products Deposited 2016-09-12	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 38–704（667 aa）	Mutation：E475Q	ZN ZINC ION × 1 CL CHLORIDE ION × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；294 K；0.1M Bis-Tris-propane, 11% PEG 3350, 10% glycerol, 0.2M potassium thiocyanate	Resolution 2.70 Å R-free 0.268
5LUZ Structure of Human Neurolysin (E475Q) in complex with neurotensin peptide products Deposited 2016-09-12	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 38–704（667 aa）	Mutation：E475Q	ZN ZINC ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；294 K；0.1M Bis-Tris-propane, 11% PEG 3350, 10% glycerol, 0.2M potassium thiocyanate	Resolution 2.70 Å R-free 0.268
5LV0 Structure of Human Neurolysin (E475Q) in complex with amyloid-beta 35-40 peptide product Deposited 2016-09-12	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 38–704（667 aa）	Mutation：E475Q	ZN ZINC ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；294 K；0.1M Bis-Tris-propane, 11% PEG 3350, 10% glycerol, 0.2M potassium thiocyanate	Resolution 2.70 Å R-free 0.260
5LV0 Structure of Human Neurolysin (E475Q) in complex with amyloid-beta 35-40 peptide product Deposited 2016-09-12	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 38–704（667 aa）	Mutation：E475Q	ZN ZINC ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；294 K；0.1M Bis-Tris-propane, 11% PEG 3350, 10% glycerol, 0.2M potassium thiocyanate	Resolution 2.70 Å R-free 0.260
8VJU Structure of Human Neurolysin in complex with dynorphin A13 peptide Deposited 2024-01-08	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 38–704（667 aa）	Not recorded	ZN ZINC ION × 2 EDO 1,2-ETHANEDIOL × 8 CL CHLORIDE ION × 1 NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；17.5 ~ 30 % polyethylene glycol 3,350 and 50 ~ 125 mM Bis-Tris HCl buffer, pH 6.5	Resolution 1.99 Å R-free 0.218
8VJV Structure of Human Neurolysin in complex with dynorphin A8(1-8) peptide Deposited 2024-01-08	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 38–704（667 aa）	Not recorded	ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 3 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；17.5 ~ 30 % polyethylene glycol 3,350 and 50 ~ 125 mM Bis-Tris HCl buffer, pH 6.5	Resolution 2.12 Å R-free 0.249
8VJW Structure of Human Neurolysin in complex with angiotensin I peptide Deposited 2024-01-08	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 38–704（667 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；17.5 ~ 30 % polyethylene glycol 3,350 and 50 ~ 125 mM Bis-Tris HCl buffer, pH 6.5	Resolution 2.49 Å R-free 0.286
8VJW Structure of Human Neurolysin in complex with angiotensin I peptide Deposited 2024-01-08	Different oligomeric state Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 38–704（667 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；17.5 ~ 30 % polyethylene glycol 3,350 and 50 ~ 125 mM Bis-Tris HCl buffer, pH 6.5	Resolution 2.49 Å R-free 0.286
8VJY Structure of Human Neurolysin in complex with Neurotensin peptide Deposited 2024-01-08	Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 38–704（667 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；17.5 ~ 30 % polyethylene glycol 3,350 and 50 ~ 125 mM Bis-Tris HCl buffer, pH 6.5	Resolution 1.95 Å R-free 0.234
8VJY Structure of Human Neurolysin in complex with Neurotensin peptide Deposited 2024-01-08	Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 38–704（667 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 10	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；17.5 ~ 30 % polyethylene glycol 3,350 and 50 ~ 125 mM Bis-Tris HCl buffer, pH 6.5	Resolution 1.95 Å R-free 0.234

6 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	NEUL_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–667； UniProt 38–704

Bradykinin

OrganismNot specified

UniProt P01042

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 381–389	Not recorded	Neurolysin, mitochondrial × 1 （Q9BYT8） ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；17.5 ~ 30 % polyethylene glycol 3,350 and 50 ~ 125 mM Bis-Tris HCl buffer, pH 6.5	Resolution 2.89 Å R-free 0.255

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 8VJX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2WOK Clavulanic acid biosynthesis oligopeptide binding protein 2 complexed with bradykinin Deposited 2009-07-26	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 381–389（9 aa）	Not recorded	GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；pH 8	Resolution 1.70 Å R-free 0.223
4ASQ Crystal structure of ANCE in complex with Bradykinin Deposited 2012-05-02	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain P 381–389（9 aa）	Not recorded	ZN ZINC ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 FLC CITRATE ANION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；100 MM HEPES 1.3 M SODIUM CITRATE, pH 7.5	Resolution 1.99 Å R-free 0.200
4ASR Crystal structure of ANCE in complex with Thr6-Bradykinin Deposited 2012-05-02	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain P 381–389（9 aa）	Mutation：YES	ZN ZINC ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 FLC CITRATE ANION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；100 MM HEPES 1.3 M SODIUM CITRATE, pH 7.5	Resolution 1.90 Å R-free 0.200
4ECB Chimeric GST Containing Inserts of Kininogen Peptides Deposited 2012-03-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 498–507（10 aa） Fragment：unp residues 1-49, kinonogen 498-507, 50-228 Chain B 498–507（10 aa） Fragment：unp residues 1-49, kinonogen 498-507, 50-228	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；100 mM HEPES, 200 mM KCl, 35% Pentaerythritol propoxylate, 0.1 M ATP solution, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.20 Å R-free 0.248
4ECC Chimeric GST Containing Inserts of Kininogen Peptides Deposited 2012-03-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 498–510（13 aa） Fragment：unp residues 1-49, kinonogen 498-510, 50-228	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；(1)0.2 M Ammonium Sulfate, 0.1 M Hepes, 25% PEG 3350 (2)0.2 M Lithium Sulfate, 25% PEG 3350, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.20 Å R-free 0.269
6F27 NMR solution structure of non-bound [des-Arg10]-kallidin (DAKD) Deposited 2017-11-23	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 380–388（9 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.6；295 K；Ionic strength (raw mmCIF value) 111；Pressure ambient NMR sample composition 3 mM DAKD, 50 mM MES, 100 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
6F3W Backbone structure of free bradykinin (BK) in DDM/CHS detergent micelle determined by MAS SSNMR Deposited 2017-11-29	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 381–389（9 aa）	Not recorded	No recorded non-water small molecule	SOLID-STATE NMR NMR measurement conditions pH 7.4；200 K；Ionic strength (raw mmCIF value) 125；Pressure 1 NMR sample composition 0.36 ug/uL [U-13C, 15N]-F8R9 Bradykinin (BK), 50 mM not labeled HEPES, 100 mM not labeled NaCl, 2 mM not labeled EDTA, 4 % w/v not labeled DDM, 100% H2O \| 100% H2O NMR sample composition 0.36 ug/uL [U-13C, 15N]-P2P3G4F5S6P7F8 Bradykinin (BK), 50 mM not labeled HEPES, 100 mM not labeled NaCl, 2 mM not labeled EDTA, 4 % w/v not labeled DDM, 100% H2O \| 100% H2O	Resolution not provided
6F3X Backbone structure of Des-Arg10-Kallidin (DAKD) peptide in frozen DDM/CHS detergent micelle solution determined by DNP-enhanced MAS SSNMR Deposited 2017-11-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 380–388（9 aa）	Not recorded	No recorded non-water small molecule	SOLID-STATE NMR NMR measurement conditions pH 7.6；110 K；Ionic strength (raw mmCIF value) 175；Pressure 1 NMR sample composition 300 uM [U-13C; U-15N] K1 Des-Arg10-Kallidin (DAKD), 10 mM not labeled AMUPOL, 50 mM not labeled HEPES, 150 mM not labeled NaCl, 4 % w/v not labeled DDM, 0.4 % w/v not labeled CHS, 10% H2O/ 40%D2O/ 50% d8-glycerol \| 10% H2O/ 40%D2O/ 50% d8-glycerol NMR sample composition 300 uM [U-13C; U-15N] R2S7 Des-Arg10-Kallidin (DAKD), 10 mM not labeled AMUPOL, 50 mM not labeled HEPES, 150 mM not labeled NaCl, 4 % w/v not labeled DDM, 0.4 % w/v not labeled CHS, 10% H2O/ 40%D2O/ 50% d8-glycerol \| 10% H2O/ 40%D2O/ 50% d8-glycerol NMR sample composition 300 uM [U-13C; U-15N] P3 Des-Arg10-Kallidin (DAKD), 10 mM not labeled AMUPOL, 50 mM not labeled HEPES, 150 mM not labeled NaCl, 4 % w/v not labeled DDM, 0.4 % w/v not labeled CHS, 10% H2O/ 40%D2O/ 50% d8-glycerol \| 10% H2O/ 40%D2O/ 50% d8-glycerol NMR sample composition 300 uM [U-13C; U-15N] P4 Des-Arg10-Kallidin (DAKD), 10 mM not labeled AMUPOL, 50 mM not labeled HEPES, 150 mM not labeled NaCl, 4 % w/v not labeled DDM, 0.4 % w/v not labeled CHS, 10% H2O/ 40%D2O/ 50% d8-glycerol \| 10% H2O/ 40%D2O/ 50% d8-glycerol NMR sample composition 300 uM [U-13C; U-15N] G5F6 Des-Arg10-Kallidin (DAKD), 10 mM not labeled AMUPOL, 50 mM not labeled HEPES, 150 mM not labeled NaCl, 4 % w/v not labeled DDM, 0.4 % w/v not labeled CHS, 10% H2O/ 40%D2O/ 50% d8-glycerol \| 10% H2O/ 40%D2O/ 50% d8-glycerol NMR sample composition 300 uM [U-13C; U-15N] S7P9 Des-Arg10-Kallidin (DAKD), 10 mM not labeled AMUPOL, 50 mM not labeled HEPES, 150 mM not labeled NaCl, 4 % w/v not labeled DDM, 0.4 % w/v not labeled CHS, 10% H2O/ 40%D2O/ 50% d8-glycerol \| 10% H2O/ 40%D2O/ 50% d8-glycerol	Resolution not provided
6F3Y Backbone structure of Des-Arg10-Kallidin (DAKD) peptide bound to human Bradykinin 1 Receptor (B1R) determined by DNP-enhanced MAS SSNMR Deposited 2017-11-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 380–388（9 aa）	Not recorded	No recorded non-water small molecule	SOLID-STATE NMR NMR measurement conditions pH 7.6；110 K；Ionic strength (raw mmCIF value) 175；Pressure 1 NMR sample composition 312.5 uM [U-13C; U-15N] K1 Des-Arg10-Kallidin (DAKD), 312.5 uM not labeled human B1R, 10 mM not labeled AMUPOL, 50 mM not labeled HEPES, 150 mM not labeled NaCl, 4 % w/v not labeled DDM, 0.4 % w/v not labeled CHS, 10% H2O/ 40%D2O/ 50% d8-glycerol \| 10% H2O/ 40%D2O/ 50% d8-glycerol NMR sample composition 312.5 uM [U-13C; U-15N] R2S7 Des-Arg10-Kallidin (DAKD), 312.5 uM not labeled human B1R, 10 mM not labeled AMUPOL, 50 mM not labeled HEPES, 150 mM not labeled NaCl, 4 % w/v not labeled DDM, 0.4 % w/v not labeled CHS, 10% H2O/ 40%D2O/ 50% d8-glycerol \| 10% H2O/ 40%D2O/ 50% d8-glycerol NMR sample composition 312.5 uM [U-13C; U-15N] P3 Des-Arg10-Kallidin (DAKD), 312.5 uM not labeled human B1R, 10 mM not labeled AMUPOL, 50 mM not labeled HEPES, 150 mM not labeled NaCl, 4 % w/v not labeled DDM, 0.4 % w/v not labeled CHS, 10% H2O/ 40%D2O/ 50% d8-glycerol \| 10% H2O/ 40%D2O/ 50% d8-glycerol NMR sample composition 312.5 uM [U-13C; U-15N] P4 Des-Arg10-Kallidin (DAKD), 312.5 uM not labeled human B1R, 10 mM not labeled AMUPOL, 50 mM not labeled HEPES, 150 mM not labeled NaCl, 4 % w/v not labeled DDM, 0.4 % w/v not labeled CHS, 10% H2O/ 40%D2O/ 50% d8-glycerol \| 10% H2O/ 40%D2O/ 50% d8-glycerol NMR sample composition 312.5 uM [U-13C; U-15N] G5F6 Des-Arg10-Kallidin (DAKD), 312.5 uM not labeled human B1R, 10 mM not labeled AMUPOL, 50 mM not labeled HEPES, 150 mM not labeled NaCl, 4 % w/v not labeled DDM, 0.4 % w/v not labeled CHS, 10% H2O/ 40%D2O/ 50% d8-glycerol \| 10% H2O/ 40%D2O/ 50% d8-glycerol NMR sample composition 312.5 uM [U-13C; U-15N] S7P9 Des-Arg10-Kallidin (DAKD), 312.5 uM not labeled human B1R, 10 mM not labeled AMUPOL, 50 mM not labeled HEPES, 150 mM not labeled NaCl, 4 % w/v not labeled DDM, 0.4 % w/v not labeled CHS, 10% H2O/ 40%D2O/ 50% d8-glycerol \| 10% H2O/ 40%D2O/ 50% d8-glycerol	Resolution not provided
7QOT Factor XI and Plasma Kallikrein apple domain structures reveals different kininogen bound complexes Deposited 2021-12-28	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 583–613（31 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；288 K；0.1M Tris pH8, 1.5M AMMONIUM SULFATE	Resolution 3.24 Å R-free 0.284
7QOT Factor XI and Plasma Kallikrein apple domain structures reveals different kininogen bound complexes Deposited 2021-12-28	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 583–613（31 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；288 K；0.1M Tris pH8, 1.5M AMMONIUM SULFATE	Resolution 3.24 Å R-free 0.284
7QOX Factor XI and Plasma Kallikrein apple domain structures reveals different kininogen bound complexes Deposited 2021-12-29	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 582–609（28 aa）	Not recorded	GOL GLYCEROL × 1 PEG DI(HYDROXYETHYL)ETHER × 3 PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1 PG4 TETRAETHYLENE GLYCOL × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；288 K；Morpheus screen H9 condition: 0.1M amino acids, 0.1M buffer system 3 pH8.5, 30% precipitant mix 1.	Resolution 2.32 Å R-free 0.253
7QOX Factor XI and Plasma Kallikrein apple domain structures reveals different kininogen bound complexes Deposited 2021-12-29	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 582–609（28 aa）	Not recorded	GOL GLYCEROL × 5 PEG DI(HYDROXYETHYL)ETHER × 2 PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 PG6 1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；288 K；Morpheus screen H9 condition: 0.1M amino acids, 0.1M buffer system 3 pH8.5, 30% precipitant mix 1.	Resolution 2.32 Å R-free 0.253

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

View Construct and Data Evidence

UniProt name	KNG1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–9； UniProt 381–389

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	8vjx
Deposition date deposition_date	2024-01-08
最后修订 last_revision	2024-08-21
Structure title title	Structure of Human Neurolysin in complex with bradykinin peptide
Keywords keywords	metallopeptidase, bioactive peptides, HYDROLASE; HYDROLASE
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	26.39 Å
Radius of gyration Rg (electron density) rg_electron	25.35 Å
Forward intensity I(0) i0	94932000.00
Molecular weight molecular_weight	77015.0 kDa
Excluded volume excluded_volume	96510 Å³
Envelope volume envelope_volume	115530 Å³
Hydration-shell volume shell_volume	36755 Å³
Envelope diameter envelope_diameter	92.1 Å
Shell Rg shell_rg	33.83 Å
Envelope Rg envelope_rg	25.35 Å
Shape Rg shape_rg	25.32 Å
Total Rg total_rg	26.29 Å
Total atoms total_atoms	5406
Residues n_residues	671
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	86.4 Å
Rg (real space) rg_real	26.25 Å
Rg uncertainty (real space) rg_real_error	0.47 Å
I(0) (real space) i0_real	9.4930e+07
I(0) uncertainty (real space) i0_real_error	1.3710e+06
Rg (reciprocal space) rg_reciprocal	26.30 Å
I(0) (reciprocal space) i0_reciprocal	94930000.0000
Solution quality estimate total_estimate	0.8746
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	33.1 Å
Skewness Skewness skewness	0.249
Kurtosis Kurtosis kurtosis	-0.216
Angular range angular_range	— – 0.3000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	22720000.0000
Real-space data points n_real_points	61
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.801; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.968

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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	Neurolysin, mitochondrial
Molecular weight formula_weight	76612.5 kDa
EC 编号 ec_number	3.4.24.16
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	5443

SSYTVAGRNVLRWDLSPEQIKTRTEELIVQTKQVYDAVGMLGIEEVTYENCLQALADVEVKYIVERTMLDFPQHVSSDKEVRAASTEADKRLSRFDIEMSMRGDIFERIVHLQETCDLGKIKPEARRYLEKSIKMGKRNGLHLPEQVQNEIKSMKKRMSELCIDFNKNLNEDDTFLVFSKAELGALPDDFIDSLEKTDDDKYKITLKYPHYFPVMKKCCIPETRRRMEMAFNTRCKEENTIILQQLLPLRTKVAKLLGYSTHADFVLEMNTAKSTSRVTAFLDDLSQKLKPLGEAEREFILNLKKKECKDRGFEYDGKINAWDLYYYMTQTEELKYSIDQEFLKEYFPIEVVTEGLLNTYQELLGLSFEQMTDAHVWNKSVTLYTVKDKATGEVLGQFYLDLYPREGKYNHAACFGLQPGCLLPDGSRMMAVAALVVNFSQPVAGRPSLLRHDEVRTYFHEFGHVMHQICAQTDFARFSGTNVETDFVEVPSQMLENWVWDVDSLRRLSKHYKDGSPIADDLLEKLVASRLVNTGLLTLRQIVLSKVDQSLHTNTSLDAASEYAKYCSEILGVAATPGTNMPATFGHLAGGYDGQYYGYLWSEVFSMDMFYSCFKKEGIMNPEVGMKYRNLILKPGGSLDGMDMLHNFLKREPNQKAFLMSRGLHAP

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 polymer

Description description	Bradykinin
Molecular weight formula_weight	1062.2 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

RPPGFSPFR

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 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	26

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8. Citations (1)

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Unit-cell length a length_a	143.826 Å
Unit-cell length b length_b	60.510 Å
Unit-cell length c length_c	96.558 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	4

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.890 Å
Low-resolution limit resolution_low	96.560 Å
R factor r_factor	0.2249
R_work r_work	0.2233
R_free r_free	0.2554

fit	/app/data/saxs_computation/vj/8vjx/8vjx.fit
pddf	/app/data/pr_computation/vj/8vjx/8vjx.pr.out
profile	/app/data/saxs_computation/vj/8vjx/8vjx.dat

Structure of Human Neurolysin in complex with bradykinin peptide

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

Neurolysin, mitochondrial

State in the Current Structure

Other States of the Same Protein in the Database

Bradykinin

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)