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2g0u

Solution Structure of Monomeric BsaL, the Type III Secretion Needle Protein of Burkholderia pseudomallei

Method: SOLUTION NMR Dmax: 54.3 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

type III secretion system needle protein

Burkholderia pseudomallei

UniProt Q63K18

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–84 Fragment：BsaLdelta5 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7；298 K；Ionic strength (raw mmCIF value) 20mM；Pressure ambient Resolution not provided

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 2G0U Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8FVU Cryo-EM structure of human Needle/NAIP/NLRC4 (R288A) Deposited 2023-01-19 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric
Chain U 2–89（88 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å

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

View Construct and Data Evidence
UniProt name Q63K18_BURPS
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–84； UniProt 1–84

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 2g0u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2g0u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2g0u
Deposition date deposition_date2006-02-13
Structure title titleSolution Structure of Monomeric BsaL, the Type III Secretion Needle Protein of Burkholderia pseudomallei
Keywords keywordshelix-turn-helix, UNKNOWN FUNCTION; UNKNOWN FUNCTION
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier20.86 Å
Radius of gyration Rg (electron density) rg_electron20.55 Å
Forward intensity I(0) i0694165000.00
Molecular weight molecular_weight207030.0 kDa
Excluded volume excluded_volume253760 ų
Envelope volume envelope_volume117460 ų
Hydration-shell volume shell_volume34572 ų
Envelope diameter envelope_diameter110.1 Å
Shell Rg shell_rg35.35 Å
Envelope Rg envelope_rg28.88 Å
Shape Rg shape_rg20.56 Å
Total Rg total_rg21.16 Å
Total atoms total_atoms28320
Residues n_residues1840
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 dmax54.3 Å
Rg (real space) rg_real19.50 Å
Rg uncertainty (real space) rg_real_error0.10 Å
I(0) (real space) i0_real6.6140e+08
I(0) uncertainty (real space) i0_real_error6.9180e+06
Rg (reciprocal space) rg_reciprocal21.08 Å
I(0) (reciprocal space) i0_reciprocal694100000.0000
Solution quality estimate total_estimate0.6815
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary21.2 Å
Skewness Skewness skewness0.229
Kurtosis Kurtosis kurtosis-0.693
Angular range angular_range— – 0.3800 Å−1
Current regularization parameter α current_alpha2.9170
Highest regularization parameter α highest_alpha217800.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.003; Oscil: 0.996; Stabil: 0.984; Sysdev: 0.000; Positv: 1.000; Valcen: 0.919; 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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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2g0ua1
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.20 — MxiH-like
Family Family familya.2.20.1 — MxiH-like
Domain ID domain_idd2g0ua2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2g0uA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily90 —
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8. Citations (1)

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9. Files and Curves (10)