← Back to search
2ljt

C9L,C14L-LeuA

Method: SOLUTION NMR Dmax: 54.1 Å Quality: REASONABLE
▼

1. Protein Identity and Related Structures Protein Identity & Related Structures

Bacteriocin leucocin-A

Leuconostoc gelidum

UniProt P34034

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 25–61 Mutation：C9L, C14L No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7；298 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient NMR sample composition：90 % [U-2H] TFE, 10 % H2O, 0.1 % TFA, 2.6 mM DSS, trifluoroethanol/water | trifluoroethanol/water 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 2LJT Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CW6 REFINED SOLUTION STRUCTURE OF LEUCOCIN A Deposited 1999-08-25 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 25–61（37 aa） Fragment：LEUCOCIN A-UAL 187
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 2.8；298 K；Ionic strength (raw mmCIF value) 0；Pressure AMBIENT
NMR sample composition 2MM LEUCOCIN A IN 90% TFE-D3,10% H2O
Resolution not provided
2LEU HIGH RESOLUTION 1H NMR STUDY OF LEUCOCIN A IN 90% AQUEOUS TRIFLUOROETHANOL (TFE) (0.1% TFA), 18 STRUCTURES Deposited 1997-05-20 Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 25–61（37 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 2.8；299 K
Resolution not provided
2LJQ (C9S, C14S)-leucocin A Deposited 2011-09-22 Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 25–61（37 aa）
Mutation：C9S, C14S No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 0.5 mM [U-99% 13C; U-99% 15N] peptide, 100 uM DSS, trifluoroethanol/water | trifluoroethanol/water
Resolution not provided
3LEU HIGH RESOLUTION 1H NMR STUDY OF LEUCOCIN A IN DODECYLPHOSPHOCHOLINE MICELLES, 19 STRUCTURES (1:40 RATIO OF LEUCOCIN A:DPC) (0.1% TFA) Deposited 1997-05-20 Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 25–61（37 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 2.8；308 K
Resolution not provided

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LCCA_LEUGE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–37； UniProt 25–61

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 2ljt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ljt
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id2ljt
Deposition date deposition_date2011-09-23
Structure title titleC9L,C14L-LeuA
Keywords keywordsAntimicrobial peptide, ANTIMICROBIAL PROTEIN; ANTIMICROBIAL PROTEIN
Experimental Method methodSOLUTION NMR
▼

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier13.48 Å
Radius of gyration Rg (electron density) rg_electron14.02 Å
Forward intensity I(0) i092751800.00
Molecular weight molecular_weight78748.0 kDa
Excluded volume excluded_volume97714 ų
Envelope volume envelope_volume21549 ų
Hydration-shell volume shell_volume11770 ų
Envelope diameter envelope_diameter58.4 Å
Shell Rg shell_rg21.43 Å
Envelope Rg envelope_rg17.23 Å
Shape Rg shape_rg14.04 Å
Total Rg total_rg14.26 Å
Total atoms total_atoms10820
Residues n_residues740
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
▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax54.1 Å
Rg (real space) rg_real13.68 Å
Rg uncertainty (real space) rg_real_error0.80 Å
I(0) (real space) i0_real9.2750e+07
I(0) uncertainty (real space) i0_real_error1.2780e+06
Rg (reciprocal space) rg_reciprocal13.67 Å
I(0) (reciprocal space) i0_reciprocal92750000.0000
Solution quality estimate total_estimate0.7022
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary15.1 Å
Skewness Skewness skewness0.433
Kurtosis Kurtosis kurtosis-0.524
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15460.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.395; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.101; Smooth: 0.842
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▶

8. Citations (1)

▶

9. Files and Curves (10)