SAXSdb — 7qe8

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

Trypsin-1

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 24–247	Mutation：S200A	Serine protease inhibitor Kazal-type 1 × 1 （P00995） SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.4；293 K；1 ul protein solution (20 mg/mL in 20 mM HEPES, pH 7.4, 150 mM NaCl) + 1 ul well solution (15% PEG 4000, 0.3 M AS), cryo 15% PEG 4000, 0.3 M AS, 8% PEG 400	Resolution 2.90 Å R-free 0.243
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 24–247	Mutation：S200A	Serine protease inhibitor Kazal-type 1 × 1 （P00995） SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.4；293 K；1 ul protein solution (20 mg/mL in 20 mM HEPES, pH 7.4, 150 mM NaCl) + 1 ul well solution (15% PEG 4000, 0.3 M AS), cryo 15% PEG 4000, 0.3 M AS, 8% PEG 400	Resolution 2.90 Å R-free 0.243

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 7QE8	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1FXY COAGULATION FACTOR XA-TRYPSIN CHIMERA INHIBITED WITH D-PHE-PRO-ARG-CHLOROMETHYLKETONE Deposited 1998-04-22	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 127–247（121 aa）	Mutation：Q20Y, E21N, C27V	0G6 D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.8；PROTEIN WAS CRYSTALLIZED FROM 15% PEG 6K, 100 MM HEPES, PH 7.8.	Resolution 2.15 Å R-free 0.245
1TRN CRYSTAL STRUCTURE OF HUMAN TRYPSIN 1: UNEXPECTED PHOSPHORYLATION OF TYROSINE 151 Deposited 1995-03-16	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 24–247（224 aa） Chain B 24–247（224 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	ISP PHOSPHORYLISOPROPANE × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å
2RA3 Human cationic trypsin complexed with bovine pancreatic trypsin inhibitor (BPTI) Deposited 2007-09-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 24–247（224 aa） Chain B 24–247（224 aa）	Mutation：R117H, S195A Mutation：R117H, S195A	CA CALCIUM ION × 2 SO4 SULFATE ION × 24	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；0.1M Tris hydrochloride pH 8.5, 1.6M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.46 Å R-free 0.178
2RA3 Human cationic trypsin complexed with bovine pancreatic trypsin inhibitor (BPTI) Deposited 2007-09-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 24–247（224 aa） Chain B 24–247（224 aa）	Mutation：R117H, S195A Mutation：R117H, S195A	CA CALCIUM ION × 4 SO4 SULFATE ION × 48	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；0.1M Tris hydrochloride pH 8.5, 1.6M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.46 Å R-free 0.178
4WWY human cationic trypsin G193R mutant in complex with bovine pancreatic trypsin inhibitor Deposited 2014-11-12	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 24–247（224 aa） Fragment：UNP residues 24-247	Mutation：G193R, R117H	SO4 SULFATE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.2M ammonium sulfate, 0.1M sodium cacodylate trihydrate, 30% PEG-8000	Resolution 1.70 Å R-free 0.207
4WWY human cationic trypsin G193R mutant in complex with bovine pancreatic trypsin inhibitor Deposited 2014-11-12	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 24–247（224 aa） Fragment：UNP residues 24-247	Mutation：G193R, R117H	SO4 SULFATE ION × 3 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.2M ammonium sulfate, 0.1M sodium cacodylate trihydrate, 30% PEG-8000	Resolution 1.70 Å R-free 0.207
4WXV Human cationic trypsin K97D mutant in complex with bovine pancreatic trypsin inhibitor (BPTI) Deposited 2014-11-14	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 24–247（224 aa） Fragment：UNP residues 24-247	Mutation：K97D, R117H, S195A	CA CALCIUM ION × 1 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.2M ammonium sulfate, 0.1 sodium cacodylate trihydrate, 30% PEG-8000	Resolution 2.10 Å R-free 0.281
4WXV Human cationic trypsin K97D mutant in complex with bovine pancreatic trypsin inhibitor (BPTI) Deposited 2014-11-14	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 24–247（224 aa） Fragment：UNP residues 24-247	Mutation：K97D, R117H, S195A	CA CALCIUM ION × 1 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.2M ammonium sulfate, 0.1 sodium cacodylate trihydrate, 30% PEG-8000	Resolution 2.10 Å R-free 0.281
7QE9 Human cationic trypsin (TRY1) complexed with serine protease inhibitor Kazal type 1 N34S (SPINK1 N34S) Deposited 2021-12-01	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 24–247（224 aa）	Mutation：S200A	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；293 K；1 uL protein solution (20 mg/mL in 20 mM Hepes pH 7.4, 150 mM NaCl) + 1 uL well solution (15% PEG 4000, 0.3 M AS), cryo: 15% PEG 4000, 0.3 M AS, 8% PEG 400	Resolution 2.10 Å R-free 0.234
7QE9 Human cationic trypsin (TRY1) complexed with serine protease inhibitor Kazal type 1 N34S (SPINK1 N34S) Deposited 2021-12-01	Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 24–247（224 aa）	Mutation：S200A	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；293 K；1 uL protein solution (20 mg/mL in 20 mM Hepes pH 7.4, 150 mM NaCl) + 1 uL well solution (15% PEG 4000, 0.3 M AS), cryo: 15% PEG 4000, 0.3 M AS, 8% PEG 400	Resolution 2.10 Å R-free 0.234
8H3S Substrate-bound EP, polyA model Deposited 2022-10-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 16–247（232 aa）	Not recorded	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 experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 16–247（232 aa）	Not recorded	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 experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 16–247（232 aa）	Not recorded	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
8ZIY trypsinogen-EP-E574A Deposited 2024-05-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 16–247（232 aa）	Not recorded	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
8ZJ4 trypsinogen-EP-N619A Deposited 2024-05-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 16–247（232 aa）	Not recorded	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

11 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TRY1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–224； UniProt 24–247 Author chain B； PDBConstruct 1–224； UniProt 24–247

Serine protease inhibitor Kazal-type 1

Homo sapiens

UniProt P00995

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 D； UniProt 24–79	Not recorded	Trypsin-1 × 1 （P07477） SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.4；293 K；1 ul protein solution (20 mg/mL in 20 mM HEPES, pH 7.4, 150 mM NaCl) + 1 ul well solution (15% PEG 4000, 0.3 M AS), cryo 15% PEG 4000, 0.3 M AS, 8% PEG 400	Resolution 2.90 Å R-free 0.243
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 24–79	Not recorded	Trypsin-1 × 1 （P07477） SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.4；293 K；1 ul protein solution (20 mg/mL in 20 mM HEPES, pH 7.4, 150 mM NaCl) + 1 ul well solution (15% PEG 4000, 0.3 M AS), cryo 15% PEG 4000, 0.3 M AS, 8% PEG 400	Resolution 2.90 Å R-free 0.243

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 7QE8	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CGI THREE-DIMENSIONAL STRUCTURE OF THE COMPLEXES BETWEEN BOVINE CHYMOTRYPSINOGEN*A AND TWO RECOMBINANT VARIANTS OF HUMAN PANCREATIC SECRETORY TRYPSIN INHIBITOR (KAZAL-TYPE) Deposited 1991-10-08	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain I 24–79（56 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å
1CGJ THREE-DIMENSIONAL STRUCTURE OF THE COMPLEXES BETWEEN BOVINE CHYMOTRYPSINOGEN*A AND TWO RECOMBINANT VARIANTS OF HUMAN PANCREATIC SECRETORY TRYPSIN INHIBITOR (KAZAL-TYPE) Deposited 1991-10-08	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain I 24–79（56 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å
1HPT THREE-DIMENSIONAL STRUCTURE OF A RECOMBINANT VARIANT OF HUMAN PANCREATIC SECRETORY TRYPSIN INHIBITOR (KAZAL TYPE) Deposited 1992-03-27	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 24–79（56 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å
7QE9 Human cationic trypsin (TRY1) complexed with serine protease inhibitor Kazal type 1 N34S (SPINK1 N34S) Deposited 2021-12-01	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 24–79（56 aa）	Mutation：N34S	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；293 K；1 uL protein solution (20 mg/mL in 20 mM Hepes pH 7.4, 150 mM NaCl) + 1 uL well solution (15% PEG 4000, 0.3 M AS), cryo: 15% PEG 4000, 0.3 M AS, 8% PEG 400	Resolution 2.10 Å R-free 0.234
7QE9 Human cationic trypsin (TRY1) complexed with serine protease inhibitor Kazal type 1 N34S (SPINK1 N34S) Deposited 2021-12-01	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 24–79（56 aa）	Mutation：N34S	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；293 K；1 uL protein solution (20 mg/mL in 20 mM Hepes pH 7.4, 150 mM NaCl) + 1 uL well solution (15% PEG 4000, 0.3 M AS), cryo: 15% PEG 4000, 0.3 M AS, 8% PEG 400	Resolution 2.10 Å R-free 0.234

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ISK1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–56； UniProt 24–79 Author chain D； PDBConstruct 1–56； UniProt 24–79

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	7qe8
Deposition date deposition_date	2021-12-01
Structure title title	Human cationic trypsin (TRY1) complexed with serine protease inhibitor Kazal type 1 (SPINK1)
Keywords keywords	TRY1, SPINK1, serine protease, protease-inhibitor complex, catalytic triad, 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	28.76 Å
Radius of gyration Rg (electron density) rg_electron	28.09 Å
Forward intensity I(0) i0	65657300.00
Molecular weight molecular_weight	60520.0 kDa
Excluded volume excluded_volume	74502 Å³
Envelope volume envelope_volume	92062 Å³
Hydration-shell volume shell_volume	28309 Å³
Envelope diameter envelope_diameter	103.2 Å
Shell Rg shell_rg	34.27 Å
Envelope Rg envelope_rg	28.42 Å
Shape Rg shape_rg	28.05 Å
Total Rg total_rg	28.80 Å
Total atoms total_atoms	4229
Residues n_residues	557
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	96.8 Å
Rg (real space) rg_real	28.92 Å
Rg uncertainty (real space) rg_real_error	0.86 Å
I(0) (real space) i0_real	6.5660e+07
I(0) uncertainty (real space) i0_real_error	1.0360e+06
Rg (reciprocal space) rg_reciprocal	28.85 Å
I(0) (reciprocal space) i0_reciprocal	65650000.0000
Solution quality estimate total_estimate	0.8398
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	26.4 Å
Skewness Skewness skewness	0.454
Kurtosis Kurtosis kurtosis	-0.501
Angular range angular_range	— – 0.2750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	21640000.0000
Real-space data points n_real_points	56
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.742; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.736; Smooth: 0.952

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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	Trypsin-1
Molecular weight formula_weight	24121.2 kDa
EC 编号 ec_number	3.4.21.4
Mutation mutation	S200A
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	4240

IVGGYNCEENSVPYQVSLNSGYHFCGGSLINEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPQYDRKTLNNDIMLIKLSSRAVINARVSTISLPTAPPATGTKCLISGWGNTASSGADYPDELQCLDAPVLSQAKCEASYPGKITSNMFCVGFLEGGKDSCQGDAGGPVVCNGQLQGVVSWGDGCAQKNKPGVYTKVYNYVKWIKNTIAANS

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	Serine protease inhibitor Kazal-type 1
Molecular weight formula_weight	6254.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

DSLGREAKCYNELNGCTKIYDPVCGTDGNTYPNECVLCFENRKRQTSILIQKSGPC

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 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1

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7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	7qe8A01
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	7qe8A02
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	7qe8B01
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	7qe8B02
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	77.626 Å
Unit-cell length b length_b	77.626 Å
Unit-cell length c length_c	187.349 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 31 2 1
Space-group number int_tables_number	152
Crystal system crystal_system	trigonal

Resolution resolution	2.900 Å
Low-resolution limit resolution_low	45.750 Å
R factor r_factor	0.2250
R_work r_work	0.2229
R_free r_free	0.2431

fit	/app/data/saxs_computation/qe/7qe8/7qe8.fit
pddf	/app/data/pr_computation/qe/7qe8/7qe8.pr.out
profile	/app/data/saxs_computation/qe/7qe8/7qe8.dat

Human cationic trypsin (TRY1) complexed with serine protease inhibitor Kazal type 1 (SPINK1)

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

Trypsin-1

State in the Current Structure

Other States of the Same Protein in the Database

Serine protease inhibitor Kazal-type 1

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

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)