5ii4

Crystal structure of red abalone VERL repeat 1 with linker at 2.0 A resolution

Method: X-RAY DIFFRACTION Dmax: 92.7 Å Quality: GOOD

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

Maltose-binding periplasmic protein,Vitelline envelope sperm lysin receptor

Haliotis rufescens

UniProt P0AEY0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 27–393 Mutation:N4115Q, N4122T, N4142Y, N4171Q,N4115Q, N4122T, N4142Y, N4171Q,N4115Q, N4122T, N4142Y, N4171Q,N4115Q, N4122T, N4142Y, N4171Q alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 PGE TRIETHYLENE GLYCOL × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9.5;293 K;40% PEG 600, 0.1M CHES Resolution 2.00 Å R-free 0.247

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.

109 other PDB entries and 148 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECO57
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 10–376; UniProt 27–393

Maltose-binding periplasmic protein,Vitelline envelope sperm lysin receptor

Haliotis rufescens

UniProt Q8WR62

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 38–175 Mutation:N4115Q, N4122T, N4142Y, N4171Q,N4115Q, N4122T, N4142Y, N4171Q,N4115Q, N4122T, N4142Y, N4171Q,N4115Q, N4122T, N4142Y, N4171Q alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 PGE TRIETHYLENE GLYCOL × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9.5;293 K;40% PEG 600, 0.1M CHES Resolution 2.00 Å R-free 0.247

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.

6 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8WR62_HALRU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 380–517; UniProt 38–175

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 5ii4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5ii4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5ii4
Deposition date deposition_date2016-03-01
Structure title titleCrystal structure of red abalone VERL repeat 1 with linker at 2.0 A resolution
Keywords keywordsCELL ADHESION, FERTILIZATION, EGG-SPERM INTERACTION, GAMETE RECOGNITION, VITELLINE ENVELOPE, SPERM RECEPTOR; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.97
Radius of gyration Rg (electron density) rg_electron23.99
Forward intensity I(0) i044741900.00
Molecular weight molecular_weight53327.0 kDa
Excluded volume excluded_volume67366 ų
Envelope volume envelope_volume79651 ų
Hydration-shell volume shell_volume27742 ų
Envelope diameter envelope_diameter80.9
Shell Rg shell_rg31.11
Envelope Rg envelope_rg24.16
Shape Rg shape_rg23.96
Total Rg total_rg24.93
Total atoms total_atoms7481
Residues n_residues477
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 dmax92.7
Rg (real space) rg_real24.91
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real4.4740e+07
I(0) uncertainty (real space) i0_real_error7.2610e+05
Rg (reciprocal space) rg_reciprocal24.92
I(0) (reciprocal space) i0_reciprocal44740000.0000
Solution quality estimate total_estimate0.7563
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary28.0
Skewness Skewness skewness0.274
Kurtosis Kurtosis kurtosis-0.460
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha14270000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.662; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.843; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id5ii4A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II

8. Citations (5)

9. Files and Curves (10)