8yd0

CryoEM structure of M. tuberculosis ClpXP1P2 complex bound to bortezomib

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ATP-dependent Clp protease ATP-binding subunit ClpX

Mycobacterium tuberculosis H37Rv

UniProt P9WPB9

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 20 ATP-dependent Clp protease proteolytic subunit 2 × 7 (P9WPC3) ATP-dependent Clp protease proteolytic subunit 1 × 7 (P9WPC5) MAGNESIUM ION × 2 ADENOSINE-5'-TRIPHOSPHATE × 4 ADENOSINE-5'-DIPHOSPHATE × 2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE × 14 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name CLPX_MYCTU
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–355; UniProt 60–414 Author chain B; PDBConstruct 1–355; UniProt 60–414 Author chain C; PDBConstruct 1–355; UniProt 60–414 Author chain D; PDBConstruct 1–355; UniProt 60–414 Author chain E; PDBConstruct 1–355; UniProt 60–414 Author chain F; PDBConstruct 1–355; UniProt 60–414

ATP-dependent Clp protease proteolytic subunit 2

Mycobacterium tuberculosis H37Rv

UniProt P9WPC3

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 20 ATP-dependent Clp protease ATP-binding subunit ClpX × 6 (P9WPB9) ATP-dependent Clp protease proteolytic subunit 1 × 7 (P9WPC5) MAGNESIUM ION × 2 ADENOSINE-5'-TRIPHOSPHATE × 4 ADENOSINE-5'-DIPHOSPHATE × 2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE × 14 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name CLPP2_MYCTU
Isoform —
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 1–196; UniProt 15–210 Author chain I; PDBConstruct 1–196; UniProt 15–210 Author chain K; PDBConstruct 1–196; UniProt 15–210 Author chain L; PDBConstruct 1–196; UniProt 15–210 Author chain M; PDBConstruct 1–196; UniProt 15–210 Author chain N; PDBConstruct 1–196; UniProt 15–210 Author chain V; PDBConstruct 1–196; UniProt 15–210

ATP-dependent Clp protease proteolytic subunit 1

Mycobacterium tuberculosis H37Rv

UniProt P9WPC5

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 20 ATP-dependent Clp protease ATP-binding subunit ClpX × 6 (P9WPB9) ATP-dependent Clp protease proteolytic subunit 2 × 7 (P9WPC3) MAGNESIUM ION × 2 ADENOSINE-5'-TRIPHOSPHATE × 4 ADENOSINE-5'-DIPHOSPHATE × 2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE × 14 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name CLPP1_MYCTU
Isoform —
PDB entities 3
Chains and sequence ranges Author chain O; PDBConstruct 1–178; UniProt 15–192 Author chain P; PDBConstruct 1–178; UniProt 15–192 Author chain Q; PDBConstruct 1–178; UniProt 15–192 Author chain R; PDBConstruct 1–178; UniProt 15–192 Author chain S; PDBConstruct 1–178; UniProt 15–192 Author chain T; PDBConstruct 1–178; UniProt 15–192 Author chain U; PDBConstruct 1–178; UniProt 15–192

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_id8yd0
Deposition date deposition_date2024-02-18
Structure title titleCryoEM structure of M. tuberculosis ClpXP1P2 complex bound to bortezomib
Keywords keywordsMycobacterium tuberculosis, Caseinolytic protease system, Activation, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY
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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.

8yd0__assembly_1__model_1

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

Download this curve (.dat)

8yd0__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

8yd0__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)54.50 Å
Rg (electron density)54.13 Å
Total Rg54.29 Å
Atom count36147
Residues4631
Excluded volume647400 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8yd0__assembly_1__model_1 20-meric (20) 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 (7)

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7. Citations (1)