2vsz

Crystal Structure of the ELMO1 PH domain

Method: X-RAY DIFFRACTION Dmax: 103.2 Å Quality: REASONABLE

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

ENGULFMENT AND CELL MOTILITY PROTEIN 1

HOMO SAPIENS

UniProt Q92556

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 532–675 Chain B; UniProt 532–675 Fragment:PLECKSTRIN HOMOLOGY DOMAIN, RESIDUES 532-675 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.75;2.1 M SODIUM MALONATE [PH 6.75] Resolution 2.30 Å R-free 0.239

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.

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

View Construct and Data Evidence
UniProt name ELMO1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–149; UniProt 532–675 Author chain B; PDBConstruct 6–149; UniProt 532–675

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 2vsz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2vsz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2vsz
Deposition date deposition_date2008-05-01
Structure title titleCrystal Structure of the ELMO1 PH domain
Keywords keywordsAPOPTOSIS, RAC SIGNALLING, SH3-BINDING, PHAGOCYTOSIS, ELMO, DOCK180, PHOSPHOINOSITIDE BINDING, GUANINE NUCLEOTIDE EXCHANGE FACTOR; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.70
Radius of gyration Rg (electron density) rg_electron29.05
Forward intensity I(0) i017094700.00
Molecular weight molecular_weight32450.0 kDa
Excluded volume excluded_volume40942 ų
Envelope volume envelope_volume55522 ų
Hydration-shell volume shell_volume17125 ų
Envelope diameter envelope_diameter107.5
Shell Rg shell_rg33.69
Envelope Rg envelope_rg29.00
Shape Rg shape_rg29.06
Total Rg total_rg29.58
Total atoms total_atoms2284
Residues n_residues289
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 dmax103.2
Rg (real space) rg_real30.09
Rg uncertainty (real space) rg_real_error1.22
I(0) (real space) i0_real1.7090e+07
I(0) uncertainty (real space) i0_real_error2.6060e+05
Rg (reciprocal space) rg_reciprocal29.93
I(0) (reciprocal space) i0_reciprocal17090000.0000
Solution quality estimate total_estimate0.6757
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.4
Skewness Skewness skewness0.445
Kurtosis Kurtosis kurtosis-0.801
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3057000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.212; Stabil: 0.995; Sysdev: 1.000; Positv: 1.000; Valcen: 0.186; Smooth: 0.974

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id2vszA01
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily810
Domain ID domain_id2vszA02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Domain ID domain_id2vszB01
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily810
Domain ID domain_id2vszB02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

8. Citations (1)

9. Files and Curves (10)