3zfw

Crystal structure of the TPR domain of kinesin light chain 2 in complex with a tryptophan-acidic cargo peptide

Method: X-RAY DIFFRACTION Dmax: 134.7 Å Quality: REASONABLE

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

KINESIN LIGHT CHAIN 2

MUS MUSCULUS

UniProt Q91YS4

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 A; UniProt 218–480 Fragment:TPR DOMAIN, RESIDUES 218-477 PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY M MEMBER 2 × 1 (Q8IWE5) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;0.10 M MES PH 6.5, 0.2 L-PROLINE, 7% PGA Resolution 2.90 Å R-free 0.244
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 218–480 Fragment:TPR DOMAIN, RESIDUES 218-477 PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY M MEMBER 2 × 1 (Q8IWE5) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;0.10 M MES PH 6.5, 0.2 L-PROLINE, 7% PGA Resolution 2.90 Å R-free 0.244

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.

4 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q91YS4_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–263; UniProt 218–480 Author chain B; PDBConstruct 1–263; UniProt 218–480

PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY M MEMBER 2

HOMO SAPIENS

UniProt Q8IWE5

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 X; UniProt 203–212 Not recorded KINESIN LIGHT CHAIN 2 × 1 (Q91YS4) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;0.10 M MES PH 6.5, 0.2 L-PROLINE, 7% PGA Resolution 2.90 Å R-free 0.244
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain Y; UniProt 203–212 Not recorded KINESIN LIGHT CHAIN 2 × 1 (Q91YS4) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;0.10 M MES PH 6.5, 0.2 L-PROLINE, 7% PGA Resolution 2.90 Å R-free 0.244

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PKHM2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain X; PDBConstruct 22–31; UniProt 203–212 Author chain Y; PDBConstruct 22–31; UniProt 203–212

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 3zfw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3zfw
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3zfw
Deposition date deposition_date2012-12-12
Structure title titleCrystal structure of the TPR domain of kinesin light chain 2 in complex with a tryptophan-acidic cargo peptide
Keywords keywordsHYDROLASE, KINESIN-CARGO RECOGNITION, MOTOR PROTEIN, TPR DOMAIN, SALMONELLA; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.91
Radius of gyration Rg (electron density) rg_electron37.13
Forward intensity I(0) i047123200.00
Molecular weight molecular_weight53305.0 kDa
Excluded volume excluded_volume66417 ų
Envelope volume envelope_volume92690 ų
Hydration-shell volume shell_volume24500 ų
Envelope diameter envelope_diameter134.1
Shell Rg shell_rg36.01
Envelope Rg envelope_rg37.15
Shape Rg shape_rg37.15
Total Rg total_rg36.99
Total atoms total_atoms3749
Residues n_residues472
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 dmax134.7
Rg (real space) rg_real37.66
Rg uncertainty (real space) rg_real_error2.06
I(0) (real space) i0_real4.7120e+07
I(0) uncertainty (real space) i0_real_error9.0220e+05
Rg (reciprocal space) rg_reciprocal37.20
I(0) (reciprocal space) i0_reciprocal47100000.0000
Solution quality estimate total_estimate0.6948
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary21.9
Skewness Skewness skewness0.585
Kurtosis Kurtosis kurtosis-0.480
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2521000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.373; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.092; Smooth: 0.818

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id3zfwA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain
Domain ID domain_id3zfwB00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain

8. Citations (1)

9. Files and Curves (10)