1mtn

BOVINE ALPHA-CHYMOTRYPSIN:BPTI CRYSTALLIZATION

Method: X-RAY DIFFRACTION Dmax: 90.0 Å Quality: GOOD

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

ALPHA-CHYMOTRYPSIN

OrganismNot specified

UniProt P00766

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–13 Chain B; UniProt 16–146 Chain C; UniProt 149–245 Not recorded BASIC PANCREATIC TRYPSIN INHIBITOR × 1 (P00974) SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;pH 6.0 Resolution 2.80 Å R-free 0.240
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 1–13 Chain F; UniProt 16–146 Chain G; UniProt 149–245 Not recorded BASIC PANCREATIC TRYPSIN INHIBITOR × 1 (P00974) SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;pH 6.0 Resolution 2.80 Å R-free 0.240
3 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–13 Chain B; UniProt 16–146 Chain C; UniProt 149–245 Chain E; UniProt 1–13 Chain F; UniProt 16–146 Chain G; UniProt 149–245 Not recorded BASIC PANCREATIC TRYPSIN INHIBITOR × 2 (P00974) SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;pH 6.0 Resolution 2.80 Å R-free 0.240

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.

91 other PDB entries and 175 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CTRA_BOVIN
Isoform
PDB entities 1, 2, 3
Chains and sequence ranges Author chain A; PDBConstruct 1–13; UniProt 1–13 Author chain E; PDBConstruct 1–13; UniProt 1–13 Author chain B; PDBConstruct 1–131; UniProt 16–146 Author chain F; PDBConstruct 1–131; UniProt 16–146 Author chain C; PDBConstruct 1–97; UniProt 149–245 Author chain G; PDBConstruct 1–97; UniProt 149–245

BASIC PANCREATIC TRYPSIN INHIBITOR

OrganismNot specified

UniProt P00974

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 36–93 Not recorded ALPHA-CHYMOTRYPSIN × 1 (P00766) ALPHA-CHYMOTRYPSIN × 1 (P00766) ALPHA-CHYMOTRYPSIN × 1 (P00766) SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;pH 6.0 Resolution 2.80 Å R-free 0.240
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain H; UniProt 36–93 Not recorded ALPHA-CHYMOTRYPSIN × 1 (P00766) ALPHA-CHYMOTRYPSIN × 1 (P00766) ALPHA-CHYMOTRYPSIN × 1 (P00766) SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;pH 6.0 Resolution 2.80 Å R-free 0.240
3 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain D; UniProt 36–93 Chain H; UniProt 36–93 Not recorded ALPHA-CHYMOTRYPSIN × 2 (P00766) ALPHA-CHYMOTRYPSIN × 2 (P00766) ALPHA-CHYMOTRYPSIN × 2 (P00766) SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;pH 6.0 Resolution 2.80 Å R-free 0.240

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.

123 other PDB entries and 263 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BPT1_BOVIN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–58; UniProt 36–93 Author chain H; PDBConstruct 1–58; UniProt 36–93

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

SAXS profile for 1mtn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1mtn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1mtn
Deposition date deposition_date1996-03-28
Structure title titleBOVINE ALPHA-CHYMOTRYPSIN:BPTI CRYSTALLIZATION
Keywords keywordsCOMPLEX, PROTEASE INHIBITOR, TRYPSIN, HYDROLASE, SERINE, COMPLEX (HYDROLASE-INHIBITOR) COMPLEX; COMPLEX (HYDROLASE/INHIBITOR)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.11
Radius of gyration Rg (electron density) rg_electron26.62
Forward intensity I(0) i069556100.00
Molecular weight molecular_weight63551.0 kDa
Excluded volume excluded_volume78798 ų
Envelope volume envelope_volume95458 ų
Hydration-shell volume shell_volume30023 ų
Envelope diameter envelope_diameter92.0
Shell Rg shell_rg33.74
Envelope Rg envelope_rg26.54
Shape Rg shape_rg26.64
Total Rg total_rg27.26
Total atoms total_atoms4440
Residues n_residues594
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax90.0
Rg (real space) rg_real27.15
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real6.9560e+07
I(0) uncertainty (real space) i0_real_error1.0360e+06
Rg (reciprocal space) rg_reciprocal27.14
I(0) (reciprocal space) i0_reciprocal69560000.0000
Solution quality estimate total_estimate0.8831
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.0
Skewness Skewness skewness0.381
Kurtosis Kurtosis kurtosis-0.407
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18400000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.858; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.937; Smooth: 0.963

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1mtn.1
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.2 — Eukaryotic proteases
Domain ID domain_idd1mtn.2
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.2 — Eukaryotic proteases
Domain ID domain_idd1mtnd_
Class classg — Small proteins
Fold Fold foldg.8 — BPTI-like
Superfamily Superfamily superfamilyg.8.1 — BPTI-like
Family Family familyg.8.1.1 — Small Kunitz-type inhibitors & BPTI-like toxins
Domain ID domain_idd1mtnh_
Class classg — Small proteins
Fold Fold foldg.8 — BPTI-like
Superfamily Superfamily superfamilyg.8.1 — BPTI-like
Family Family familyg.8.1.1 — Small Kunitz-type inhibitors & BPTI-like toxins

CATH v4.4 (6 domains)

Domain ID domain_id1mtnB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1mtnC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1mtnD00
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology410 — Factor Xa Inhibitor
Homologous superfamily homologous superfamily10 — Pancreatic trypsin inhibitor Kunitz domain
Domain ID domain_id1mtnF00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1mtnG00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1mtnH00
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology410 — Factor Xa Inhibitor
Homologous superfamily homologous superfamily10 — Pancreatic trypsin inhibitor Kunitz domain

8. Citations (1)

9. Files and Curves (10)