3l3t

Human mesotrypsin complexed with amyloid precursor protein inhibitor variant (APPIR15K)

Method: X-RAY DIFFRACTION D_max: 119.0 Å Quality: GOOD

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

PRSS3 protein

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 28–251	Fragment：UNP residues 28-251 Mutation：S195A	Protein APP × 1 （C9JHU0） FMT FORMIC ACID × 7 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；298 K；4M sodium formate solution, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.38 Å R-free 0.237
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 28–251	Fragment：UNP residues 28-251 Mutation：S195A	Protein APP × 1 （C9JHU0） FMT FORMIC ACID × 5 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；298 K；4M sodium formate solution, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.38 Å R-free 0.237
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 28–251	Fragment：UNP residues 28-251 Mutation：S195A	Protein APP × 1 （C9JHU0） FMT FORMIC ACID × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；298 K；4M sodium formate solution, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.38 Å R-free 0.237
4	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 28–251	Fragment：UNP residues 28-251 Mutation：S195A	Protein APP × 1 （C9JHU0） CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；298 K；4M sodium formate solution, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.38 Å R-free 0.237

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 3L3T	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3P92 Human mesotrypsin complexed with bovine pancreatic trypsin inhibitor variant (BPTI-K15R/R17G) Deposited 2010-10-15	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 28–251（224 aa）	Mutation：S195A	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；25% PEG4000, 0.2M Na acetate and 100mM Tris pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.60 Å R-free 0.159
3P92 Human mesotrypsin complexed with bovine pancreatic trypsin inhibitor variant (BPTI-K15R/R17G) Deposited 2010-10-15	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 28–251（224 aa）	Mutation：S195A	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；25% PEG4000, 0.2M Na acetate and 100mM Tris pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.60 Å R-free 0.159
3P95 Human mesotrypsin complexed with bovine pancreatic trypsin inhibitor variant (BPTI-K15R/R17D) Deposited 2010-10-15	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 28–251（224 aa）	Mutation：S195A	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；25% PEG4000, 0.2M Na acetate and 100mM Tris pH 8.0, vapor diffusion, hanging drop, temperature 298K	Resolution 1.30 Å R-free 0.132
4DG4 Human mesotrypsin-S39Y complexed with bovine pancreatic trypsin inhibitor (BPTI) Deposited 2012-01-24	Different construct 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 28–251（224 aa） Fragment：unp residues 28-251	Mutation：S195A, S39Y	SO4 SULFATE ION × 5 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；1.6M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.40 Å R-free 0.211
4DG4 Human mesotrypsin-S39Y complexed with bovine pancreatic trypsin inhibitor (BPTI) Deposited 2012-01-24	Different construct 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 28–251（224 aa） Fragment：unp residues 28-251	Mutation：S195A, S39Y	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；1.6M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.40 Å R-free 0.211
4DG4 Human mesotrypsin-S39Y complexed with bovine pancreatic trypsin inhibitor (BPTI) Deposited 2012-01-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 28–251（224 aa） Fragment：unp residues 28-251	Mutation：S195A, S39Y	SO4 SULFATE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；1.6M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.40 Å R-free 0.211
4DG4 Human mesotrypsin-S39Y complexed with bovine pancreatic trypsin inhibitor (BPTI) Deposited 2012-01-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 28–251（224 aa） Fragment：unp residues 28-251	Mutation：S195A, S39Y	SO4 SULFATE ION × 10	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；1.6M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.40 Å R-free 0.211
5JBT Mesotrypsin in complex with cleaved amyloid precursor like protein 2 inhibitor (APLP2) Deposited 2016-04-13	Different construct 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 28–251（224 aa）	Mutation：S195A	CA CALCIUM ION × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.2 M Ammonium Sulfate 0.1 M Sodium Cacodylate Trihydrate 30% PEG 8000	Resolution 1.40 Å R-free 0.199
6GFI Structure of Human Mesotrypsin in complex with APPI variant T11V/M17R/I18F/F34V Deposited 2018-04-30	Different construct 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 28–251（224 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1M Sodium Chloride, 0.1M Bis-Tris pH 6.8 , 1.42M Ammonium Sulfate	Resolution 2.30 Å R-free 0.301
6GFI Structure of Human Mesotrypsin in complex with APPI variant T11V/M17R/I18F/F34V Deposited 2018-04-30	Different construct 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 28–251（224 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1M Sodium Chloride, 0.1M Bis-Tris pH 6.8 , 1.42M Ammonium Sulfate	Resolution 2.30 Å R-free 0.301
6HAR Crystal structure of Mesotrypsin in complex with APPI-M17C/I18F/F34C Deposited 2018-08-08	Different construct 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 28–251（224 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1M MES pH 6.8, 16% PEG 20, 000	Resolution 1.50 Å R-free 0.193

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

View Construct and Data Evidence

UniProt name	Q8N2U3_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–224； UniProt 28–251 Author chain B； PDBConstruct 1–224； UniProt 28–251 Author chain C； PDBConstruct 1–224； UniProt 28–251 Author chain D； PDBConstruct 1–224； UniProt 28–251

Protein APP

Homo sapiens

UniProt C9JHU0

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 E； UniProt 211–267	Fragment：UNP residues 211-267 Mutation：R15K	PRSS3 protein × 1 （Q8N2U3） FMT FORMIC ACID × 7 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；298 K；4M sodium formate solution, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.38 Å R-free 0.237
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain F； UniProt 211–267	Fragment：UNP residues 211-267 Mutation：R15K	PRSS3 protein × 1 （Q8N2U3） FMT FORMIC ACID × 5 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；298 K；4M sodium formate solution, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.38 Å R-free 0.237
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain G； UniProt 211–267	Fragment：UNP residues 211-267 Mutation：R15K	PRSS3 protein × 1 （Q8N2U3） FMT FORMIC ACID × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；298 K；4M sodium formate solution, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.38 Å R-free 0.237
4	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain H； UniProt 211–267	Fragment：UNP residues 211-267 Mutation：R15K	PRSS3 protein × 1 （Q8N2U3） CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；298 K；4M sodium formate solution, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.38 Å R-free 0.237

Other States of the Same Protein in the Database

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	C9JHU0_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 1–57； UniProt 211–267 Author chain F； PDBConstruct 1–57； UniProt 211–267 Author chain G； PDBConstruct 1–57； UniProt 211–267 Author chain H； PDBConstruct 1–57； UniProt 211–267

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3l3t
Deposition date deposition_date	2009-12-17
Structure title title	Human mesotrypsin complexed with amyloid precursor protein inhibitor variant (APPIR15K)
Keywords keywords	;Human mesotrypsin, Canonical inhibitor, Alzheimer's amyloid precursor protein inhibitor, APPI, APPI-R15K, Hydrolase-Cell Adhesion complex ;; Hydrolase/Cell Adhesion
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	36.88 Å
Radius of gyration Rg (electron density) rg_electron	36.30 Å
Forward intensity I(0) i0	247123000.00
Molecular weight molecular_weight	122650.0 kDa
Excluded volume excluded_volume	151480 Å³
Envelope volume envelope_volume	200380 Å³
Hydration-shell volume shell_volume	46536 Å³
Envelope diameter envelope_diameter	125.1 Å
Shell Rg shell_rg	41.82 Å
Envelope Rg envelope_rg	36.07 Å
Shape Rg shape_rg	36.29 Å
Total Rg total_rg	36.69 Å
Total atoms total_atoms	8579
Residues n_residues	1112
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	119.0 Å
Rg (real space) rg_real	36.75 Å
Rg uncertainty (real space) rg_real_error	0.75 Å
I(0) (real space) i0_real	2.4710e+08
I(0) uncertainty (real space) i0_real_error	3.7330e+06
Rg (reciprocal space) rg_reciprocal	36.84 Å
I(0) (reciprocal space) i0_reciprocal	247100000.0000
Solution quality estimate total_estimate	0.8979
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	52.6 Å
Skewness Skewness skewness	0.121
Kurtosis Kurtosis kurtosis	-0.593
Angular range angular_range	— – 0.2150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	24820000.0000
Real-space data points n_real_points	44
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.915; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.934

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	PRSS3 protein
Molecular weight formula_weight	24257.5 kDa
EC 编号 ec_number	3.4.21.4
Mutation mutation	S195A
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	8967

IVGGYTCEENSLPYQVSLNSGSHFCGGSLISEQWVVSAAHCYKTRIQVRLGEHNIKVLEGNEQFINAAKIIRHPKYNRDTLDNDIMLIKLSSPAVINARVSTISLPTAPPAAGTECLISGWGNTLSFGADYPDELKCLDAPVLTQAECKASYPGKITNSMFCVGFLEGGKDSCQRDAGGPVVCNGQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDTIAANS

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	Protein APP
Molecular weight formula_weight	6249.0 kDa
Mutation mutation	R15K
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,F,G,H

EVCSEQAETGPCKAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAI

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	Pichia pastoris

Entity 3 Entity 3 non-polymer

Description description	FORMIC ACID
Molecular weight formula_weight	46.0 kDa
Source method src_method	syn
Copy count entity_count	13

Entity 4 Entity 4 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	345

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7. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d3l3ta_
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

Domain ID domain_id	d3l3tb_
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

Domain ID domain_id	d3l3tc_
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

Domain ID domain_id	d3l3td_
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

Domain ID domain_id	d3l3te_
Class class	g — Small proteins
Fold Fold fold	g.8 — BPTI-like
Superfamily Superfamily superfamily	g.8.1 — BPTI-like
Family Family family	g.8.1.1 — Small Kunitz-type inhibitors & BPTI-like toxins

Domain ID domain_id	d3l3tf_
Class class	g — Small proteins
Fold Fold fold	g.8 — BPTI-like
Superfamily Superfamily superfamily	g.8.1 — BPTI-like
Family Family family	g.8.1.1 — Small Kunitz-type inhibitors & BPTI-like toxins

Domain ID domain_id	d3l3tg_
Class class	g — Small proteins
Fold Fold fold	g.8 — BPTI-like
Superfamily Superfamily superfamily	g.8.1 — BPTI-like
Family Family family	g.8.1.1 — Small Kunitz-type inhibitors & BPTI-like toxins

Domain ID domain_id	d3l3th_
Class class	g — Small proteins
Fold Fold fold	g.8 — BPTI-like
Superfamily Superfamily superfamily	g.8.1 — BPTI-like
Family Family family	g.8.1.1 — Small Kunitz-type inhibitors & BPTI-like toxins

CATH v4.4 (12 domains)

Domain ID domain_id	3l3tA01
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	3l3tA02
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	3l3tB01
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	3l3tB02
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	3l3tC01
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	3l3tC02
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	3l3tD01
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	3l3tD02
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	3l3tE00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	410 — Factor Xa Inhibitor
Homologous superfamily homologous superfamily	10 — Pancreatic trypsin inhibitor Kunitz domain

Domain ID domain_id	3l3tF00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	410 — Factor Xa Inhibitor
Homologous superfamily homologous superfamily	10 — Pancreatic trypsin inhibitor Kunitz domain

Domain ID domain_id	3l3tG00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	410 — Factor Xa Inhibitor
Homologous superfamily homologous superfamily	10 — Pancreatic trypsin inhibitor Kunitz domain

Domain ID domain_id	3l3tH00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	410 — Factor Xa Inhibitor
Homologous superfamily homologous superfamily	10 — Pancreatic trypsin inhibitor Kunitz domain

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8. Citations (1)

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Unit-cell length a length_a	92.793 Å
Unit-cell length b length_b	130.067 Å
Unit-cell length c length_c	132.338 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	16

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

Resolution resolution	2.378 Å
Low-resolution limit resolution_low	24.515 Å
R factor r_factor	—
R_work r_work	0.1830
R_free r_free	0.2370

fit	/app/data/saxs_computation/l3/3l3t/3l3t.fit
pddf	/app/data/pr_computation/l3/3l3t/3l3t.pr.out
profile	/app/data/saxs_computation/l3/3l3t/3l3t.dat

Human mesotrypsin complexed with amyloid precursor protein inhibitor variant (APPIR15K)

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

PRSS3 protein

State in the Current Structure

Other States of the Same Protein in the Database

Protein APP

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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (8 domains)

CATH v4.4 (12 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)