9y9c

Cryo-EM map of the in vitro reconstituted RAZR:GP77 complex with AlphaFold-predicted models fitted into the density.

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

Gp77

Escherichia phage SECphi27

UniProt A0AAE8YXX1

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 48 DUF4145 domain-containing protein × 24 (A0A0F3V1L6) ZINC ION × 24 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name A0AAE8YXX1_9CAUD
Isoform —
PDB entities 1
Chains and sequence ranges Author chain IA; PDBConstruct 1–217; UniProt 1–217 Author chain IB; PDBConstruct 1–217; UniProt 1–217 Author chain IC; PDBConstruct 1–217; UniProt 1–217 Author chain ID; PDBConstruct 1–217; UniProt 1–217 Author chain IE; PDBConstruct 1–217; UniProt 1–217 Author chain IF; PDBConstruct 1–217; UniProt 1–217 Author chain IG; PDBConstruct 1–217; UniProt 1–217 Author chain IH; PDBConstruct 1–217; UniProt 1–217 Author chain II; PDBConstruct 1–217; UniProt 1–217 Author chain IJ; PDBConstruct 1–217; UniProt 1–217 Author chain IK; PDBConstruct 1–217; UniProt 1–217 Author chain IL; PDBConstruct 1–217; UniProt 1–217 Author chain IM; PDBConstruct 1–217; UniProt 1–217 Author chain IN; PDBConstruct 1–217; UniProt 1–217 Author chain IO; PDBConstruct 1–217; UniProt 1–217 Author chain IP; PDBConstruct 1–217; UniProt 1–217 Author chain IQ; PDBConstruct 1–217; UniProt 1–217 Author chain IR; PDBConstruct 1–217; UniProt 1–217 Author chain IS; PDBConstruct 1–217; UniProt 1–217 Author chain IT; PDBConstruct 1–217; UniProt 1–217 Author chain IU; PDBConstruct 1–217; UniProt 1–217 Author chain IV; PDBConstruct 1–217; UniProt 1–217 Author chain IW; PDBConstruct 1–217; UniProt 1–217 Author chain IX; PDBConstruct 1–217; UniProt 1–217

DUF4145 domain-containing protein

Escherichia coli

UniProt A0A0F3V1L6

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 48 Gp77 × 24 (A0AAE8YXX1) ZINC ION × 24 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name A0A0F3V1L6_ECOLX
Isoform —
PDB entities 2
Chains and sequence ranges Author chain OA; PDBConstruct 1–219; UniProt 1–219 Author chain OB; PDBConstruct 1–219; UniProt 1–219 Author chain OC; PDBConstruct 1–219; UniProt 1–219 Author chain OD; PDBConstruct 1–219; UniProt 1–219 Author chain OE; PDBConstruct 1–219; UniProt 1–219 Author chain OF; PDBConstruct 1–219; UniProt 1–219 Author chain OG; PDBConstruct 1–219; UniProt 1–219 Author chain OH; PDBConstruct 1–219; UniProt 1–219 Author chain OI; PDBConstruct 1–219; UniProt 1–219 Author chain OJ; PDBConstruct 1–219; UniProt 1–219 Author chain OK; PDBConstruct 1–219; UniProt 1–219 Author chain OL; PDBConstruct 1–219; UniProt 1–219 Author chain OM; PDBConstruct 1–219; UniProt 1–219 Author chain ON; PDBConstruct 1–219; UniProt 1–219 Author chain OO; PDBConstruct 1–219; UniProt 1–219 Author chain OP; PDBConstruct 1–219; UniProt 1–219 Author chain OQ; PDBConstruct 1–219; UniProt 1–219 Author chain OR; PDBConstruct 1–219; UniProt 1–219 Author chain OS; PDBConstruct 1–219; UniProt 1–219 Author chain OT; PDBConstruct 1–219; UniProt 1–219 Author chain OU; PDBConstruct 1–219; UniProt 1–219 Author chain OV; PDBConstruct 1–219; UniProt 1–219 Author chain OW; PDBConstruct 1–219; UniProt 1–219 Author chain OX; PDBConstruct 1–219; UniProt 1–219

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_id9y9c
Deposition date deposition_date2025-09-14
Structure title titleCryo-EM map of the in vitro reconstituted RAZR:GP77 complex with AlphaFold-predicted models fitted into the density.
Keywords keywordsPhage-bacterial defense complex, Abortive infection Ring-Activated Zinc-Finger RNase (RAZR), RNA BINDING PROTEIN; RNA BINDING PROTEIN
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.

9y9c__assembly_1__model_1

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

Download this curve (.dat)

9y9c__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.

9y9c__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)98.05 Å
Rg (electron density)97.78 Å
Total Rg98.09 Å
Atom count112779
Residues7248
Excluded volume1008600 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9y9c__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)