SAXSdb — 8h3u

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

Enteropeptidase non-catalytic heavy chain

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 183–784 Chain B； UniProt 785–1019	Mutation：H825A,D876A,S971A	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 4.70 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 8H3U	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4DGJ Structure of a human enteropeptidase light chain variant Deposited 2012-01-26	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 785–1019（235 aa）	Mutation：N6D, G21D, G22D, C112S, N142D, K210E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；292 K；0.1 M HEPES, 16% PEG 10000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 1.90 Å R-free 0.210
4DGJ Structure of a human enteropeptidase light chain variant Deposited 2012-01-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 785–1019（235 aa）	Mutation：N6D, G21D, G22D, C112S, N142D, K210E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；292 K；0.1 M HEPES, 16% PEG 10000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 1.90 Å R-free 0.210
4DGJ Structure of a human enteropeptidase light chain variant Deposited 2012-01-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 785–1019（235 aa）	Mutation：N6D, G21D, G22D, C112S, N142D, K210E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；292 K；0.1 M HEPES, 16% PEG 10000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 1.90 Å R-free 0.210
4DGJ Structure of a human enteropeptidase light chain variant Deposited 2012-01-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 785–1019（235 aa）	Mutation：N6D, G21D, G22D, C112S, N142D, K210E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；292 K；0.1 M HEPES, 16% PEG 10000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 1.90 Å R-free 0.210
6ZOV ENTEROPEPTIDASE IN COMPLEX WITH COMPOUND 6 Deposited 2020-07-07	Different construct Different mutation/modification 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 785–1019（235 aa） Fragment：CATALYTIC DOMAIN	Not recorded	GBS 4-carbamimidamidobenzoic acid × 1 PGE TRIETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.25；293 K；PEG20000	Resolution 2.19 Å R-free 0.250
6ZOV ENTEROPEPTIDASE IN COMPLEX WITH COMPOUND 6 Deposited 2020-07-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 785–1019（235 aa） Fragment：CATALYTIC DOMAIN	Not recorded	GBS 4-carbamimidamidobenzoic acid × 1 EDO 1,2-ETHANEDIOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.25；293 K；PEG20000	Resolution 2.19 Å R-free 0.250
6ZOV ENTEROPEPTIDASE IN COMPLEX WITH COMPOUND 6 Deposited 2020-07-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 785–1019（235 aa） Fragment：CATALYTIC DOMAIN	Not recorded	GBS 4-carbamimidamidobenzoic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.25；293 K；PEG20000	Resolution 2.19 Å R-free 0.250
6ZOV ENTEROPEPTIDASE IN COMPLEX WITH COMPOUND 6 Deposited 2020-07-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 785–1019（235 aa） Fragment：CATALYTIC DOMAIN	Not recorded	GBS 4-carbamimidamidobenzoic acid × 1 EDO 1,2-ETHANEDIOL × 2 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.25；293 K；PEG20000	Resolution 2.19 Å R-free 0.250
7WQW Structure of Active-EP Deposited 2022-01-26	Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 524–784（261 aa） Chain B 785–1019（235 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
7WQX Structure of Inactive-EP Deposited 2022-01-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 519–1019（501 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å
7WQZ Structure of Active-mutEP Deposited 2022-01-26	Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 524–784（261 aa） Chain B 785–1019（235 aa）	Mutation：H825A, D876A, S971A	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
7WR7 Structure of Inhibited-EP Deposited 2022-01-26	Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 524–784（261 aa） Chain B 785–1019（235 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 GBS 4-carbamimidamidobenzoic acid × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
8H3S Substrate-bound EP, polyA model Deposited 2022-10-09	Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 183–784（602 aa） Chain B 785–1019（235 aa）	Mutation：H825A, D876A, S971A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.90 Å
8ZI4 Cryo-EM structure of wtEP-trypsinogen Deposited 2024-05-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 182–784（603 aa） Chain D 785–1019（235 aa）	Mutation：H825A/D876A/S971A	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.95 Å
8ZIV wtEP-trypsinogen in Tryp-1 Deposited 2024-05-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 182–784（603 aa） Chain D 785–1019（235 aa）	Mutation：H825A/D876A/S971A	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.95 Å
8ZIW enteropeptidase with E574A Deposited 2024-05-14	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 501–784（284 aa） Chain D 785–1019（235 aa）	Mutation：E574A Mutation：H825A/D876A/S971A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.92 Å
8ZIY trypsinogen-EP-E574A Deposited 2024-05-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 182–784（603 aa） Chain D 785–1019（235 aa）	Mutation：E574A Mutation：H825A/D876A/S971A	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.64 Å
8ZIZ enteropeptidase with N619A Deposited 2024-05-14	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 509–784（276 aa） Chain D 785–1019（235 aa）	Mutation：N619A Mutation：H825A/D876A/S971A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.89 Å
8ZJ4 trypsinogen-EP-N619A Deposited 2024-05-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 182–784（603 aa） Chain D 785–1019（235 aa）	Mutation：N619A Mutation：H825A/D876A/S971A	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.67 Å

13 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ENTK_HUMAN
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 1–602； UniProt 183–784 Author chain B； PDBConstruct 1–235； UniProt 785–1019

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	8h3u
Deposition date deposition_date	2022-10-09
Structure title title	Inhibitor-bound EP, polyA model
Keywords keywords	complex, membrane protein; MEMBRANE PROTEIN
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	42.23 Å
Radius of gyration Rg (electron density) rg_electron	42.40 Å
Forward intensity I(0) i0	131253000.00
Molecular weight molecular_weight	90759.0 kDa
Excluded volume excluded_volume	112360 Å³
Envelope volume envelope_volume	165000 Å³
Hydration-shell volume shell_volume	34256 Å³
Envelope diameter envelope_diameter	151.5 Å
Shell Rg shell_rg	44.50 Å
Envelope Rg envelope_rg	41.64 Å
Shape Rg shape_rg	42.31 Å
Total Rg total_rg	42.82 Å
Total atoms total_atoms	6383
Residues n_residues	818
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	143.2 Å
Rg (real space) rg_real	42.67 Å
Rg uncertainty (real space) rg_real_error	1.56 Å
I(0) (real space) i0_real	1.3130e+08
I(0) uncertainty (real space) i0_real_error	2.4670e+06
Rg (reciprocal space) rg_reciprocal	42.24 Å
I(0) (reciprocal space) i0_reciprocal	131200000.0000
Solution quality estimate total_estimate	0.7890
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	30.9 Å
Skewness Skewness skewness	0.473
Kurtosis Kurtosis kurtosis	-0.571
Angular range angular_range	— – 0.1850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	8196000.0000
Real-space data points n_real_points	38
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.699; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.603; Smooth: 0.551

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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	Enteropeptidase non-catalytic heavy chain
Molecular weight formula_weight	66652.9 kDa
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	6383

ECLPGSSPCTDALTCIKADLFCDGEVNCPDGSDEDNKMCATVCDGRFLLTGSSGSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYYTDILDIYEGVGSSKILRASIWETNPGTIRIFSNQVTATFLIESDESDYVGFNATYTAFNSSELNNYEKINCNFEDGFCFWVQDLNDDNEWERIQGSTFSPFTGPNFDHTFGNASGFYISTPTGPGGRQERVGLLSLPLDPTLEPACLSFWYHMYGENVHKLSINISNDQNMEKTVFQKEGNYGDNWNYGQVTLNETVKFKVAFNAFKNKILSDIALDDISLTYGICNGSLYPEPTLVPTPPPELPTDCGGPFELWEPNTTFSSTNFPNSYPNLAFCVWILNAQKGKNIQLHFQEFDLENINDVVEIRDGEEADSLLLAVYTGPGPVKDVFSTTNRMTVLLITNDVLARGGFKANFTTGYHLGIPEPCKADHFQCKNGECVPLVNLCDGHLHCEDGSDEADCVRFFNGTTNNNGLVRFRIQSIWHTACAENWTTQISNDVCQLLGLGSGNSSKPIFPTDGGPFVKLNTAPDGHLILTPSQQCLQDSLIRLQCNHKSCGKKLAAQDITPK

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	Enteropeptidase catalytic light chain
Molecular weight formula_weight	26277.8 kDa
Mutation mutation	H825A,D876A,S971A
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

IVGGSNAKEGAWPWVVGLYYGGRLLCGASLVSSDWLVSAAHCVYGRNLEPSKWTAILGLHMKSNLTSPQTVPRLIDEIVINPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWGTVVYQGTTANILQEADVPLLSNERCQQQMPEYNITENMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLAGVTSFGYKCALPNRPGVYARVSRFTEWIQSFLH

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	—

Resolution resolution	4.70 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	119676

fit	/app/data/saxs_computation/h3/8h3u/8h3u.fit
pddf	/app/data/pr_computation/h3/8h3u/8h3u.pr.out
profile	/app/data/saxs_computation/h3/8h3u/8h3u.dat

Inhibitor-bound EP, polyA model

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

Enteropeptidase non-catalytic heavy chain

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)