SAXSdb — 1eax

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

SUPPRESSOR OF TUMORIGENICITY 14

HOMO SAPIENS

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 615–855	Fragment：CATALYTIC RESIDUES 615-855	SO4 SULFATE ION × 1 BEN BENZAMIDINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；pH 8.00	Resolution 1.30 Å R-free 0.193

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 1EAX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1EAW Crystal structure of the MTSP1 (matriptase)-BPTI (aprotinin) complex Deposited 2001-07-17	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 615–855（241 aa） Fragment：CATALYTIC RESIDUES 615-855	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；pH 8.00	Resolution 2.93 Å R-free 0.279
1EAW Crystal structure of the MTSP1 (matriptase)-BPTI (aprotinin) complex Deposited 2001-07-17	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 615–855（241 aa） Fragment：CATALYTIC RESIDUES 615-855	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；pH 8.00	Resolution 2.93 Å R-free 0.279
2GV6 Crystal Structure of Matriptase with Inhibitor CJ-730 Deposited 2006-05-02	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 615–855（241 aa）	Not recorded	730 (S)-3-(3-(4-(2-GUANIDINOETHYL)PIPERIDIN-1-YL)-2-(NAPHTHALENE-2-SULFONAMIDO)-3-OXOPROPYL)BENZIMIDAMIDE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.10 Å R-free 0.229
2GV7 Structure of Matriptase in Complex with Inhibitor CJ-672 Deposited 2006-05-02	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 615–855（241 aa）	Not recorded	672 (S)-4-(4-(3-(3-CARBAMIMIDOYLPHENYL)-2-(2,4,6-TRIISOPROPYLPHENYLSULFONAMIDO)PROPANOYL)PIPERAZINE-1-CARBONYL)PIPERIDINE-1-CARBOXIMIDAMIDE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å R-free 0.238
3BN9 Crystal Structure of MT-SP1 in complex with Fab Inhibitor E2 Deposited 2007-12-13	Different construct 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 B 615–855（241 aa） Fragment：Peptidase S1 domain	Mutation：C122S	EDO 1,2-ETHANEDIOL × 9 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；293 K；16% PEG 5000 MME, 0.21M AmSO4, 0.1M Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.17 Å R-free 0.267
3BN9 Crystal Structure of MT-SP1 in complex with Fab Inhibitor E2 Deposited 2007-12-13	Different construct 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 A 615–855（241 aa） Fragment：Peptidase S1 domain	Mutation：C122S	EDO 1,2-ETHANEDIOL × 4 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；293 K；16% PEG 5000 MME, 0.21M AmSO4, 0.1M Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.17 Å R-free 0.267
3NCL Crystal Structure of MT-SP1 bound to Benzamidine Phosphonate Inhibitor Deposited 2010-06-04	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 615–855（241 aa） Fragment：peptidase S1 domain	Mutation：C731S	CCZ phenyl (4-carbamimidoylbenzyl)phosphonate × 1 FMT FORMIC ACID × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；4.0 M Na Formate, 25mM FeCl3, 20% glycerol cryoprotectant, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.19 Å R-free 0.156
3NPS Crystal structure of membrane-type serine protease 1 (MT-SP1) in complex with the Fab Inhibitor S4 Deposited 2010-06-29	Different construct 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 615–855（241 aa） Fragment：PEPTIDASE S1 DOMAIN (unp residues 615-855)	Mutation：C122S	EDO 1,2-ETHANEDIOL × 10 NA SODIUM ION × 5 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions 298 K；50 mM Tris, 100 mM NaCl, 5% glycerol, no buffer was added for crystallization, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.50 Å R-free 0.228
3SO3 Structures of Fab-Protease Complexes Reveal a Highly Specific Non-Canonical Mechanism of Inhibition. Deposited 2011-06-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 615–855（241 aa） Fragment：PEPTIDASE S1 DOMAIN	Mutation：YES	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；16% PEG 3350, 0.23 M MgSO4, 0.4% isopropanol, 3% glycerol, 0.12 M AMSO4, vapor diffusion, hanging drop, temperature 293k, VAPOR DIFFUSION, HANGING DROP	Resolution 2.10 Å R-free 0.194
4IS5 Crystal Structure of the ligand-free inactive Matriptase Deposited 2013-01-16	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 615–855（241 aa） Fragment：serine protease domain (unp resisdues 615-855)	Mutation：N164Q, S195A	SO4 SULFATE ION × 4 GOL GLYCEROL × 3 GSH Glutathione × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；295 K；0.1 M Tris-HCL , pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 1.48 Å R-free 0.179
4IS5 Crystal Structure of the ligand-free inactive Matriptase Deposited 2013-01-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 615–855（241 aa） Fragment：serine protease domain (unp resisdues 615-855)	Mutation：N164Q, S195A	SO4 SULFATE ION × 8 GOL GLYCEROL × 6 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；295 K；0.1 M Tris-HCL , pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 1.48 Å R-free 0.179
4ISL Crystal Structure of the inactive Matriptase in complex with its inhibitor HAI-1 Deposited 2013-01-16	Different construct Different mutation/modification 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 615–855（241 aa） Fragment：Serine protease domain (unp residues 615-855)	Mutation：N164Q, S805A	PG4 TETRAETHYLENE GLYCOL × 1 GOL GLYCEROL × 3 PGE TRIETHYLENE GLYCOL × 1 GSH Glutathione × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；295 K；0.1 M Tris-HCl, 20% (w/v) polyethylene glycol 8000, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.29 Å R-free 0.232
4ISN Crystal Structure of Matriptase in complex with its inhibitor HAI-1 Deposited 2013-01-16	Different construct Different mutation/modification 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 615–855（241 aa） Fragment：Serine protease domain (UNP RESIDUES 615-855)	Mutation：N164Q	PG4 TETRAETHYLENE GLYCOL × 1 GSH Glutathione × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；295 K；0.1 M Tris-HCl pH 8.5, 20% (w/v) polyethylene glycol 8000, vapor diffusion, sitting drop, temperature 295K	Resolution 2.45 Å R-free 0.259
4ISO Crystal Structure of Matriptase in complex with its inhibitor HAI-1 Deposited 2013-01-16	Different construct Different mutation/modification 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 615–855（241 aa） Fragment：serine protease domain (UNP RESIDUES 615-855)	Mutation：N164Q	GSH Glutathione × 1 GOL GLYCEROL × 2 PEG DI(HYDROXYETHYL)ETHER × 4 PGE TRIETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；295 K；0.1 M Tris-HCl, 20% (w/v) polyethylene glycol 8000 , pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.01 Å R-free 0.219
4JYT Crystal Structure of Matriptase in complex with Inhibitor Deposited 2013-04-01	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 615–855（241 aa） Fragment：UNP residues 615-855	Not recorded	N4A 4,4'-[{3-[(naphthalen-2-ylsulfonyl)amino]pyridine-2,6-diyl}bis(oxy)]dibenzenecarboximidamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.3；291 K；0.1M Tris, 0.2M MgCl2, 20% PEG8000 , pH 8.3, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.00 Å R-free 0.248
4JZ1 Crystal Structure of Matriptase in complex with Inhibitor Deposited 2013-04-02	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 615–855（241 aa） Fragment：UNP residues 615-855	Not recorded	F4D 4,4'-[(3-{[(4-fluorophenyl)sulfonyl]amino}pyridine-2,6-diyl)bis(oxy)]dibenzenecarboximidamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.3；291 K；0.1M Tris pH 8.3 0.2M MgCl2, 20% PEG8000, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.90 Å R-free 0.241
4JZI Crystal Structure of Matriptase in complex with Inhibitor". Deposited 2013-04-03	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 615–855（241 aa） Fragment：UNP residues 615-855	Not recorded	N4C N-(trans-4-aminocyclohexyl)-2,6-bis(4-carbamimidoylphenoxy)pyridine-4-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.3；291 K；0.1M Tris pH 8.3 0.2M MgCl2, 20% PEG8000, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.00 Å R-free 0.244
4O97 Crystal structure of matriptase in complex with inhibitor Deposited 2014-01-02	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 615–855（241 aa） Fragment：UNP RESIDUES 615-855 Chain B 604–607（4 aa） Fragment：UNP RESIDUES 604-607	Not recorded	NTX N-(trans-4-aminocyclohexyl)-3,5-bis[(3-carbamimidoylbenzyl)oxy]benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.3；293 K；0.1M Tris pH 8.3, 0.2M MgCl2, 20% PEG 8000 , VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.20 Å R-free 0.277
4O9V Crystal structure of matriptase in complex with inhibitor Deposited 2014-01-03	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 615–855（241 aa） Fragment：UNP RESIDUES 615-855 Chain B 604–607（4 aa） Fragment：UNP RESIDUES 604-607	Not recorded	NT4 N-(trans-4-aminocyclohexyl)-3,5-bis(4-carbamimidoylphenoxy)benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.3；293 K；0.1M Tris pH 8.3 0.2M MgCl2, 20% PEG 8000 , VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.90 Å R-free 0.239
4R0I CRYSTAL STRUCTURE of MATRIPTASE in COMPLEX WITH INHIBITOR Deposited 2014-07-31	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 615–855（241 aa） Fragment：UNP residues 615-855 Chain B 604–607（4 aa） Fragment：UNP residues 604-607	Not recorded	3KM 3-({(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[(naphthalen-2-ylsulfonyl)amino]-3-oxopropyl}oxy)benzenecarboximidamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.3；293 K；0.1M Tris pH 8.3 0.2M MgCl2, 20% PEG8000 , VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.90 Å R-free 0.289
5LYO Crystal structure of the zymogen matriptase catalytic domain Deposited 2016-09-28	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 604–855（252 aa）	Not recorded	SO4 SULFATE ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M MES 6.5, 2.0 M ammonium sulfate	Resolution 2.50 Å R-free 0.263
5LYO Crystal structure of the zymogen matriptase catalytic domain Deposited 2016-09-28	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 604–855（252 aa）	Not recorded	SO4 SULFATE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M MES 6.5, 2.0 M ammonium sulfate	Resolution 2.50 Å R-free 0.263
5LYO Crystal structure of the zymogen matriptase catalytic domain Deposited 2016-09-28	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 604–855（252 aa）	Not recorded	SO4 SULFATE ION × 9	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M MES 6.5, 2.0 M ammonium sulfate	Resolution 2.50 Å R-free 0.263
6N4T Crystal structure of Matriptase1 in complex with a peptidomimetic benzothiazole Deposited 2018-11-20	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 615–855（241 aa）	Not recorded	MG MAGNESIUM ION × 1 EOH ETHANOL × 1 GSH Glutathione × 1 KD7 N-(3-phenylpropanoyl)-3-(1,3-thiazol-4-yl)-L-alanyl-N-[(1S,2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-hydroxypentan-2-yl]-L-valinamide × 1 144 TRIS-HYDROXYMETHYL-METHYL-AMMONIUM × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；0.1 M Tris, pH 8.2 - 8.7, 18 % - 22 % PEG800, 200 mM MgCl2	Resolution 1.95 Å R-free 0.225
6T9T Matriptase in complex with the synthetic inhibitor (S)-3-(3-(4-(3-(tert-butyl)ureido)piperidin-1-yl)-2-((3'-fluoro-4'-(hydroxymethyl)-[1,1'-biphenyl])-3-sulfonamido)-3-oxopropyl)benzimidamide (MI-1904) Deposited 2019-10-28	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 615–855（241 aa）	Not recorded	CL CHLORIDE ION × 1 MXH 1-~{tert}-butyl-3-[1-[(2~{S})-3-(3-carbamimidoylphenyl)-2-[[3-[3-fluoranyl-4-(hydroxymethyl)phenyl]phenyl]sulfonylamino ]propanoyl]piperidin-4-yl]urea × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；291 K；100 mM Sodium acetate pH 4.6, 2 M Sodium formate, protein concentration 7 mg/ml	Resolution 1.69 Å R-free 0.202
8G1V Crystal Structure Matriptase (C731S) in Complex with Inhibitor MM1132-2 Deposited 2023-02-03	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 615–855（241 aa） Fragment：residues 615-855	Mutation：C731S	SO4 SULFATE ION × 4 CL CHLORIDE ION × 5 GOL GLYCEROL × 2 YIL N~2~-{[3-(acetamidomethyl)phenyl]acetyl}-N-[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1,1-dihydroxypentan-2-yl]-L-leucinamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；2M ammonium sulfate, 100 sodium cacodylate, 200 mM NaCl	Resolution 1.35 Å R-free 0.152
8G1W Crystal Structure Matriptase (C731S) in Complex with Inhibitor VD4162B Deposited 2023-02-03	Different construct 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 615–855（241 aa） Fragment：residues 615-855	Mutation：C731S	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；291 K；2M sodium formate, 100 sodium acetate	Resolution 1.20 Å R-free 0.166

22 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ST14_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–241； UniProt 615–855

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	1eax
Deposition date deposition_date	2001-07-17
Structure title title	Crystal structure of MTSP1 (matriptase)
Keywords keywords	HYDROLASE, SERINE PROTEINASE, MATRIX DEGRADATION; 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	17.82 Å
Radius of gyration Rg (electron density) rg_electron	16.59 Å
Forward intensity I(0) i0	13353900.00
Molecular weight molecular_weight	26648.0 kDa
Excluded volume excluded_volume	33030 Å³
Envelope volume envelope_volume	36948 Å³
Hydration-shell volume shell_volume	18077 Å³
Envelope diameter envelope_diameter	54.3 Å
Shell Rg shell_rg	23.37 Å
Envelope Rg envelope_rg	16.94 Å
Shape Rg shape_rg	16.58 Å
Total Rg total_rg	17.68 Å
Total atoms total_atoms	1878
Residues n_residues	241
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	52.2 Å
Rg (real space) rg_real	17.64 Å
Rg uncertainty (real space) rg_real_error	0.06 Å
I(0) (real space) i0_real	1.2870e+07
I(0) uncertainty (real space) i0_real_error	1.1410e+05
Rg (reciprocal space) rg_reciprocal	17.69 Å
I(0) (reciprocal space) i0_reciprocal	13350000.0000
Solution quality estimate total_estimate	0.7154
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	22.6 Å
Skewness Skewness skewness	0.098
Kurtosis Kurtosis kurtosis	-0.442
Angular range angular_range	— – 0.4450 Å⁻¹
Current regularization parameter α current_alpha	11.0000
Highest regularization parameter α highest_alpha	4030000.0000
Real-space data points n_real_points	75
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.949; Stabil: 0.914; Sysdev: 0.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.752

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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	SUPPRESSOR OF TUMORIGENICITY 14
Molecular weight formula_weight	26463.8 kDa
EC 编号 ec_number	3.4.21.-
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	2259

VVGGTDADEGEWPWQVSLHALGQGHICGASLISPNWLVSAAHCYIDDRGFRYSDPTQWTAFLGLHDQSQRSAPGVQERRLKRIISHPFFNDFTFDYDIALLELEKPAEYSSMVRPICLPDASHVFPAGKAIWVTGWGHTQYGGTGALILQKGEIRVINQTTCENLLPQQITPRMMCVGFLSGGVDSCQGDSGGPLSSVEADGRIFQAGVVSWGDGCAQRNKPGVYTRLPLFRDWIKENTGV

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	SACCHAROMYCES CEREVISIAE

Entity 2 Entity 2 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	BENZAMIDINE
Molecular weight formula_weight	120.2 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	381

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1eaxa_
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.2 — Eukaryotic proteases

CATH v4.4 (2 domains)

Domain ID domain_id	1eaxA01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

Domain ID domain_id	1eaxA02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

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8. Citations (1)

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Unit-cell length a length_a	66.918 Å
Unit-cell length b length_b	141.604 Å
Unit-cell length c length_c	51.936 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	8

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

Resolution resolution	1.300 Å
Low-resolution limit resolution_low	17.750 Å
R factor r_factor	0.1840
R_work r_work	0.1840
R_free r_free	0.1930

fit	/app/data/saxs_computation/ea/1eax/1eax.fit
pddf	/app/data/pr_computation/ea/1eax/1eax.pr.out
profile	/app/data/saxs_computation/ea/1eax/1eax.dat

Crystal structure of MTSP1 (matriptase)

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

SUPPRESSOR OF TUMORIGENICITY 14

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