1v49

Solution structure of microtubule-associated protein light chain-3

Method: SOLUTION NMR Dmax: 50.4 Å Quality: GOOD

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

Microtubule-associated proteins 1A/1B light chain 3B

Homo sapiens

UniProt Q9GZQ8

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 0–119 Fragment:residues 1-120 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 230;Pressure 1 NMR sample composition:0.8mM protein U-15N, 13C; 25mM phosphate buffer NA; 100mM NACL; 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:0.8mM protein U-15N, 13C; 25mM phosphate buffer NA; 100mM NACL; 100% D2O | 100% D2O 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.

49 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MLP3B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–120; UniProt 0–119

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 1v49

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1v49
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1v49
Deposition date deposition_date2003-11-11
Structure title titleSolution structure of microtubule-associated protein light chain-3
Keywords keywordsUBIQUITIN FOLD, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier16.08
Radius of gyration Rg (electron density) rg_electron14.47
Forward intensity I(0) i03924660.00
Molecular weight molecular_weight14130.0 kDa
Excluded volume excluded_volume17833 ų
Envelope volume envelope_volume21183 ų
Hydration-shell volume shell_volume12514 ų
Envelope diameter envelope_diameter49.1
Shell Rg shell_rg20.08
Envelope Rg envelope_rg14.77
Shape Rg shape_rg14.44
Total Rg total_rg15.75
Total atoms total_atoms2007
Residues n_residues120
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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 dmax50.4
Rg (real space) rg_real15.97
Rg uncertainty (real space) rg_real_error0.21
I(0) (real space) i0_real3.9250e+06
I(0) uncertainty (real space) i0_real_error4.1890e+04
Rg (reciprocal space) rg_reciprocal15.98
I(0) (reciprocal space) i0_reciprocal3925000.0000
Solution quality estimate total_estimate0.8969
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.8
Skewness Skewness skewness0.099
Kurtosis Kurtosis kurtosis-0.421
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha724100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.894; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.978

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1v49a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.3 — GABARAP-like

CATH v4.4 (1 domains)

Domain ID domain_id1v49A00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)