2bya

Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CATIONIC TRYPSIN

OrganismNot specified

UniProt P00760

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 BENZAMIDINE × 1 GLYCEROL × 1 SULFATE ION × 2 CALCIUM ION × 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name TRY1_BOVIN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain X; PDBConstruct 1–39; UniProt 1–39 Author chain X; PDBConstruct 40–70; UniProt 40–70 Author chain X; PDBConstruct 71–127; UniProt 71–127 Author chain X; PDBConstruct 128–131; UniProt 128–131 Author chain X; PDBConstruct 132–184; UniProt 132–184 Author chain X; PDBConstruct 185–189; UniProt 185–189 Author chain X; PDBConstruct 190–206; UniProt 190–206 Author chain X; PDBConstruct 207–215; UniProt 207–215 Author chain X; PDBConstruct 216–218; UniProt 216–218 Author chain X; PDBConstruct 219–243; UniProt 219–243

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_id2bya
Deposition date deposition_date2005-07-29
Structure title titleIs radiation damage dependent on the dose-rate used during macromolecular crystallography data collection
Keywords keywordsDATA COLLECTION, RADIATION DAMAGE, DOSE-RATE, SYNCHROTRON RADIATION, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

2bya__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2bya__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

2bya__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)17.36 Å
Rg (electron density)16.12 Å
Total Rg17.19 Å
Atom count1655
Residues223
Excluded volume29284 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2bya__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (6)

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6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2byax_
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

CATH v4.4 (2 domains)

Domain ID domain_id2byaX01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2byaX02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
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7. Citations (1)