1pa7

Crystal structure of amino-terminal microtubule binding domain of EB1

Method: X-RAY DIFFRACTION Dmax: 46.0 Å Quality: GOOD

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

Microtubule-associated protein RP/EB family member 1

Homo sapiens

UniProt Q15691

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 1–130 Fragment:N-terminal domain, EB1 microtubule-binding domain SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;298 K;PEG4K, ammonium sulfate, MES, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 1.45 Å R-free 0.189

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.

31 other PDB entries and 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MARE1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–130; UniProt 1–130

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 1pa7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1pa7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1pa7
Deposition date deposition_date2003-05-13
Structure title titleCrystal structure of amino-terminal microtubule binding domain of EB1
Keywords keywordsCH domain, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.34
Radius of gyration Rg (electron density) rg_electron13.75
Forward intensity I(0) i04430450.00
Molecular weight molecular_weight15209.0 kDa
Excluded volume excluded_volume19161 ų
Envelope volume envelope_volume21170 ų
Hydration-shell volume shell_volume12833 ų
Envelope diameter envelope_diameter44.8
Shell Rg shell_rg19.79
Envelope Rg envelope_rg14.05
Shape Rg shape_rg13.70
Total Rg total_rg15.17
Total atoms total_atoms1068
Residues n_residues130
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 dmax46.0
Rg (real space) rg_real15.17
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real4.4300e+06
I(0) uncertainty (real space) i0_real_error4.8760e+04
Rg (reciprocal space) rg_reciprocal15.19
I(0) (reciprocal space) i0_reciprocal4430000.0000
Solution quality estimate total_estimate0.8774
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.1
Skewness Skewness skewness-0.033
Kurtosis Kurtosis kurtosis-0.454
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1432000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.849; Stabil: 0.994; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.902

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1pa7a_
Class classa — All alpha proteins
Fold Fold folda.40 — CH domain-like
Superfamily Superfamily superfamilya.40.1 — Calponin-homology domain, CH-domain
Family Family familya.40.1.1 — Calponin-homology domain, CH-domain

CATH v4.4 (1 domains)

Domain ID domain_id1pa7A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily10 — Calponin-like domain

8. Citations (1)

9. Files and Curves (10)