1zl8

NMR structure of L27 heterodimer from C. elegans Lin-7 and H. sapiens Lin-2 scaffold proteins

Method: SOLUTION NMR Dmax: 54.0 Å Quality: REASONABLE

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

Peripheral plasma membrane protein CASK

Homo sapiens

UniProt O14936

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 403–456 Fragment:L27 domain LIN-7 × 1 SOLUTION NMR NMR measurement conditions:pH 8;298 K;Ionic strength (raw mmCIF value) 0;Pressure ambient NMR sample composition:2mM Lin-7/Lin-2C; 20mM HEPES, 5mM TCEP, 0.05% DSS, 0.05% sodium azide, 90% H2O, 10% D2O | 90% D2O, 10% 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.

21 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSKP_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–54; UniProt 403–456

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 1zl8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1zl8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1zl8
Deposition date deposition_date2005-05-05
Structure title titleNMR structure of L27 heterodimer from C. elegans Lin-7 and H. sapiens Lin-2 scaffold proteins
Keywords keywordsheterodimer, L27, alpha helix, scaffold, assembly, specificity, signaling, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.18
Radius of gyration Rg (electron density) rg_electron14.56
Forward intensity I(0) i0222190000.00
Molecular weight molecular_weight122210.0 kDa
Excluded volume excluded_volume151830 ų
Envelope volume envelope_volume25636 ų
Hydration-shell volume shell_volume13757 ų
Envelope diameter envelope_diameter57.0
Shell Rg shell_rg21.85
Envelope Rg envelope_rg17.04
Shape Rg shape_rg14.58
Total Rg total_rg14.71
Total atoms total_atoms17100
Residues n_residues1070
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 dmax54.0
Rg (real space) rg_real15.21
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real2.2220e+08
I(0) uncertainty (real space) i0_real_error2.9280e+06
Rg (reciprocal space) rg_reciprocal15.21
I(0) (reciprocal space) i0_reciprocal222200000.0000
Solution quality estimate total_estimate0.7479
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.4
Skewness Skewness skewness0.391
Kurtosis Kurtosis kurtosis-0.171
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha306100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.604; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.905; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1zl8a1
Class classa — All alpha proteins
Fold Fold folda.194 — L27 domain
Superfamily Superfamily superfamilya.194.1 — L27 domain
Family Family familya.194.1.1 — L27 domain
Domain ID domain_idd1zl8a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1zl8b1
Class classa — All alpha proteins
Fold Fold folda.194 — L27 domain
Superfamily Superfamily superfamilya.194.1 — L27 domain
Family Family familya.194.1.1 — L27 domain

CATH v4.4 (2 domains)

Domain ID domain_id1zl8A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily650 — L27 domain
Domain ID domain_id1zl8B00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily650 — L27 domain

8. Citations (1)

9. Files and Curves (10)