2y9j

THREE-DIMENSIONAL MODEL OF SALMONELLA'S NEEDLE COMPLEX AT SUBNANOMETER RESOLUTION

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

PROTEIN PRGH

OrganismNot specified

UniProt P41783

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 48 LIPOPROTEIN PRGK × 24 (P41786) water × 24 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name PRGH_SALTY
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–186; UniProt 177–362 Author chain B; PDBConstruct 1–186; UniProt 177–362 Author chain C; PDBConstruct 1–186; UniProt 177–362 Author chain D; PDBConstruct 1–186; UniProt 177–362 Author chain E; PDBConstruct 1–186; UniProt 177–362 Author chain F; PDBConstruct 1–186; UniProt 177–362 Author chain G; PDBConstruct 1–186; UniProt 177–362 Author chain H; PDBConstruct 1–186; UniProt 177–362 Author chain I; PDBConstruct 1–186; UniProt 177–362 Author chain J; PDBConstruct 1–186; UniProt 177–362 Author chain K; PDBConstruct 1–186; UniProt 177–362 Author chain L; PDBConstruct 1–186; UniProt 177–362 Author chain M; PDBConstruct 1–186; UniProt 177–362 Author chain N; PDBConstruct 1–186; UniProt 177–362 Author chain O; PDBConstruct 1–186; UniProt 177–362 Author chain P; PDBConstruct 1–186; UniProt 177–362 Author chain Q; PDBConstruct 1–186; UniProt 177–362 Author chain R; PDBConstruct 1–186; UniProt 177–362 Author chain S; PDBConstruct 1–186; UniProt 177–362 Author chain T; PDBConstruct 1–186; UniProt 177–362 Author chain U; PDBConstruct 1–186; UniProt 177–362 Author chain V; PDBConstruct 1–186; UniProt 177–362 Author chain W; PDBConstruct 1–186; UniProt 177–362 Author chain X; PDBConstruct 1–186; UniProt 177–362

LIPOPROTEIN PRGK

OrganismNot specified

UniProt P41786

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 48 PROTEIN PRGH × 24 (P41783) water × 24 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name PRGK_SALTY
Isoform —
PDB entities 2
Chains and sequence ranges Author chain Y; PDBConstruct 1–170; UniProt 21–190 Author chain Z; PDBConstruct 1–170; UniProt 21–190 Author chain a; PDBConstruct 1–170; UniProt 21–190 Author chain b; PDBConstruct 1–170; UniProt 21–190 Author chain c; PDBConstruct 1–170; UniProt 21–190 Author chain d; PDBConstruct 1–170; UniProt 21–190 Author chain e; PDBConstruct 1–170; UniProt 21–190 Author chain f; PDBConstruct 1–170; UniProt 21–190 Author chain g; PDBConstruct 1–170; UniProt 21–190 Author chain h; PDBConstruct 1–170; UniProt 21–190 Author chain i; PDBConstruct 1–170; UniProt 21–190 Author chain j; PDBConstruct 1–170; UniProt 21–190 Author chain k; PDBConstruct 1–170; UniProt 21–190 Author chain l; PDBConstruct 1–170; UniProt 21–190 Author chain m; PDBConstruct 1–170; UniProt 21–190 Author chain n; PDBConstruct 1–170; UniProt 21–190 Author chain o; PDBConstruct 1–170; UniProt 21–190 Author chain p; PDBConstruct 1–170; UniProt 21–190 Author chain q; PDBConstruct 1–170; UniProt 21–190 Author chain r; PDBConstruct 1–170; UniProt 21–190 Author chain s; PDBConstruct 1–170; UniProt 21–190 Author chain t; PDBConstruct 1–170; UniProt 21–190 Author chain u; PDBConstruct 1–170; UniProt 21–190 Author chain v; PDBConstruct 1–170; UniProt 21–190

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_id2y9j
Deposition date deposition_date2011-02-15
Structure title titleTHREE-DIMENSIONAL MODEL OF SALMONELLA'S NEEDLE COMPLEX AT SUBNANOMETER RESOLUTION
Keywords keywordsPROTEIN TRANSPORT, TYPE III SECRETION, IR1, INNER MEMBRANE RING, C24-FOLD; PROTEIN TRANSPORT
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.

2y9j__assembly_1__model_1

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

Download this curve (.dat)

2y9j__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 108 109 1010 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

2y9j__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)94.56 Å
Rg (electron density)94.31 Å
Total Rg94.38 Å
Atom count69120
Residues8544
Excluded volume1226600 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2y9j__assembly_1__model_1 48-meric (48) 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)