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1btz

Episelection: novel KI ~nanomolar inhibitors of serine proteases selected by binding or chemistry on an enzyme surface

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

BETA-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 N-(tert-butoxycarbonyl)-L-alanyl-N-{(1R)-5-ammonio-1-[hydroxy(methoxy)boranyl]pentyl}-L-valinamide × 1 CALCIUM ION × 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

Monomer
1auj 1az8 1bju 1bjv 1btp 1btw 1btx 1bty 1btz 1c1n 1c1o 1c1p

521 assemblies; showing the first 12

Homodimer
3pmj 5gxp

2 assemblies

Homotetramer

None

Other homooligomers

None

Heteromeric or nucleic-acid complex
1aq7 1c9t 1c9t 1c9t 1c9t 1c9t 1c9t 1d6r 1ejm 1ejm 1ejm 1ezx

248 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name TRY1_BOVIN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–229； UniProt 15–243

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_id1btz
Deposition date deposition_date1995-05-17
Structure title titleEpiselection: novel KI ~nanomolar inhibitors of serine proteases selected by binding or chemistry on an enzyme surface
Keywords keywordsTRIPEPTIDEBORONATE METHYL ESTER INHIBITED, SERINE PROTEINASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX; HYDROLASE/HYDROLASE INHIBITOR
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.

1btz__assembly_1__model_1

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

Download this curve (.dat)

1btz__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.

1btz__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）17.18 Å
Rg (electron density)16.08 Å
Total Rg17.10 Å
Atom count2046
Residues223
Excluded volume29300 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1btz__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 (4)

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6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1btza_
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_id1btzA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1btzA02
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 (6)