8esi

Bile Salt Hydrolase from B. longum with covalent inhibitor bound

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

Conjugated bile acid hydrolase

Bifidobacterium longum

UniProt Q9KK62

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 4 ;(1R,3aS,3bR,5aR,7R,9aS,9bS,11aR)-1-[(2R)-6-fluoro-5-oxohexan-2-yl]-9a,11a-dimethylhexadecahydro-1H-cyclopenta[a]phenanthren-7-yl hydrogen sulfate (non-preferred name) ; × 4 water × 4 Consistent with protein count
2 Protein homooligomer Homooligomer Protein 4 ;(1R,3aS,3bR,5aR,7R,9aS,9bS,11aR)-1-[(2R)-6-fluoro-5-oxohexan-2-yl]-9a,11a-dimethylhexadecahydro-1H-cyclopenta[a]phenanthren-7-yl hydrogen sulfate (non-preferred name) ; × 4 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name CBH_BIFLN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–317; UniProt 1–317 Author chain B; PDBConstruct 1–317; UniProt 1–317 Author chain C; PDBConstruct 1–317; UniProt 1–317 Author chain D; PDBConstruct 1–317; UniProt 1–317 Author chain E; PDBConstruct 1–317; UniProt 1–317 Author chain F; PDBConstruct 1–317; UniProt 1–317 Author chain G; PDBConstruct 1–317; UniProt 1–317 Author chain H; PDBConstruct 1–317; UniProt 1–317

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_id8esi
Deposition date deposition_date2022-10-14
Structure title titleBile Salt Hydrolase from B. longum with covalent inhibitor bound
Keywords keywordsbile salt hydrolase, 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.

8esi__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

8esi__assembly_2__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

8esi__assembly_2__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)34.28 Å
Rg (electron density)33.71 Å
Total Rg34.11 Å
Atom count9588
Residues1259
Excluded volume167780 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8esi__assembly_1__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 8esi__assembly_2__model_1 tetrameric (4) 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 (3)

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7. Citations (1)