2x9b

The filamentous phages fd and IF1 use different infection mechanisms

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

ATTACHMENT PROTEIN G3P

ENTEROBACTERIA PHAGE IF1

UniProt O80297

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 water × 1 Consistent with protein count
2 Protein monomer Monomer Protein 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name G3P_BPIF1
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–65; UniProt 17–81 Author chain B; PDBConstruct 1–65; UniProt 17–81

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_id2x9b
Deposition date deposition_date2010-03-15
Structure title titleThe filamentous phages fd and IF1 use different infection mechanisms
Keywords keywordsVIRION, VIRAL PROTEIN, PHAGE RECOGNITION, HOST PHAGE COAT PROTEIN HOST-VIRUS INTERACTION; VIRAL PROTEIN
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.

2x9b__assembly_2__model_1

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

Download this curve (.dat)

2x9b__assembly_2__model_1 | I(q)

10-2 10-1 104 105 106 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

2x9b__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)12.27 Å
Rg (electron density)11.06 Å
Total Rg12.47 Å
Atom count473
Residues61
Excluded volume8169 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2x9b__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 2x9b__assembly_2__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 (2)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2x9ba_
Class classb — All beta proteins
Fold Fold foldb.37 — N-terminal domains of the minor coat protein g3p
Superfamily Superfamily superfamilyb.37.1 — N-terminal domains of the minor coat protein g3p
Family Family familyb.37.1.0 — automated matches
Domain ID domain_idd2x9bb_
Class classb — All beta proteins
Fold Fold foldb.37 — N-terminal domains of the minor coat protein g3p
Superfamily Superfamily superfamilyb.37.1 — N-terminal domains of the minor coat protein g3p
Family Family familyb.37.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id2x9bA00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology27 — Phage FD Coat Protein, Membrane penetration domain
Homologous superfamily homologous superfamily10 — Phage FD Coat Protein,Membrane penetration domain
Domain ID domain_id2x9bB00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology27 — Phage FD Coat Protein, Membrane penetration domain
Homologous superfamily homologous superfamily10 — Phage FD Coat Protein,Membrane penetration domain
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7. Citations (1)