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9mgh

In situ cryo-EM structure of bacteriophage Ur-lambda tail side fiber

Method: ELECTRON MICROSCOPY Dmax: 147.9 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Tail fiber protein

Escherichia phage Lambda

UniProt P03764

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 12 PDB declaration: 12-meric（12） Consistent with protein copy count Chain Ta； UniProt 1–94 Chain Tb； UniProt 1–94 Chain Tc； UniProt 1–94 Chain Td； UniProt 1–94 Chain Te； UniProt 1–94 Chain Tf； UniProt 1–94 Chain Tg； UniProt 1–94 Chain Th； UniProt 1–94 Chain Ti； UniProt 1–94 Chain Tj； UniProt 1–94 Chain Tk； UniProt 1–94 Chain Tl； UniProt 1–94 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.31 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 9MGH Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
9E7M In situ cryoEM structure of bacteriophage Ur-lambda tail tip complex Deposited 2024-11-03 Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric
Chain Ta 1–94（94 aa）
Chain Tb 1–94（94 aa）
Chain Tc 1–94（94 aa）
Chain Td 1–94（94 aa）
Chain Te 1–94（94 aa）
Chain Tf 1–94（94 aa）
Chain Tg 1–94（94 aa）
Chain Th 1–94（94 aa）
Chain Ti 1–94（94 aa）
Chain Tj 1–94（94 aa）
Chain Tk 1–94（94 aa）
Chain Tl 1–94（94 aa）
Not recorded SF4 IRON/SULFUR CLUSTER × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.37 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIBER_LAMBD
Isoform —
PDB entities 1
Chains and sequence ranges Author chain Ta； PDBConstruct 1–94； UniProt 1–94 Author chain Tb； PDBConstruct 1–94； UniProt 1–94 Author chain Tc； PDBConstruct 1–94； UniProt 1–94 Author chain Td； PDBConstruct 1–94； UniProt 1–94 Author chain Te； PDBConstruct 1–94； UniProt 1–94 Author chain Tf； PDBConstruct 1–94； UniProt 1–94 Author chain Tg； PDBConstruct 1–94； UniProt 1–94 Author chain Th； PDBConstruct 1–94； UniProt 1–94 Author chain Ti； PDBConstruct 1–94； UniProt 1–94 Author chain Tj； PDBConstruct 1–94； UniProt 1–94 Author chain Tk； PDBConstruct 1–94； UniProt 1–94 Author chain Tl； PDBConstruct 1–94； UniProt 1–94

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.

SAXS scattering curve SAXS Profile

SAXS profile for 9mgh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9mgh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9mgh
Deposition date deposition_date2024-12-10
最后修订 last_revision2025-11-26
Structure title titleIn situ cryo-EM structure of bacteriophage Ur-lambda tail side fiber
Keywords keywordsbacteriophage, tail tip complex, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier55.49 Å
Radius of gyration Rg (electron density) rg_electron54.84 Å
Forward intensity I(0) i0225219000.00
Molecular weight molecular_weight120770.0 kDa
Excluded volume excluded_volume149360 ų
Envelope volume envelope_volume301770 ų
Hydration-shell volume shell_volume45605 ų
Envelope diameter envelope_diameter139.0 Å
Shell Rg shell_rg64.51 Å
Envelope Rg envelope_rg48.71 Å
Shape Rg shape_rg54.80 Å
Total Rg total_rg55.26 Å
Total atoms total_atoms8448
Residues n_residues1128
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax147.9 Å
Rg (real space) rg_real55.21 Å
Rg uncertainty (real space) rg_real_error0.99 Å
I(0) (real space) i0_real2.2520e+08
I(0) uncertainty (real space) i0_real_error4.1160e+06
Rg (reciprocal space) rg_reciprocal55.68 Å
I(0) (reciprocal space) i0_reciprocal225400000.0000
Solution quality estimate total_estimate0.6788
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary100.4 Å
Skewness Skewness skewness-0.320
Kurtosis Kurtosis kurtosis-1.105
Angular range angular_range— – 0.1400 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4824000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.342; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.794; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)