4gla

OBody NL8 bound to hen egg-white lysozyme

Method: X-RAY DIFFRACTION Dmax: 86.8 Å Quality: GOOD

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

Lysozyme C

OrganismNot specified

UniProt P00698

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 19–147 Fragment:UNP residues 19-147 OBody NL8 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.3;291 K;0.2 M HEPES, 7% MPEG5000, pH 7.3, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 2.75 Å R-free 0.296
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 19–147 Fragment:UNP residues 19-147 OBody NL8 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.3;291 K;0.2 M HEPES, 7% MPEG5000, pH 7.3, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 2.75 Å R-free 0.296

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.

1320 other PDB entries and 1449 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LYSC_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–129; UniProt 19–147 Author chain B; PDBConstruct 1–129; UniProt 19–147

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 4gla

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4gla
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4gla
Deposition date deposition_date2012-08-14
Structure title titleOBody NL8 bound to hen egg-white lysozyme
Keywords keywords;beta barrel, OB-fold, protein-protein complex, novel scaffold, muraminidase, enzyme inhibition, engineered binding protein, HYDROLASE-DE NOVO PROTEIN complex ;; HYDROLASE/DE NOVO PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.56
Radius of gyration Rg (electron density) rg_electron26.60
Forward intensity I(0) i039753700.00
Molecular weight molecular_weight47450.0 kDa
Excluded volume excluded_volume58937 ų
Envelope volume envelope_volume74351 ų
Hydration-shell volume shell_volume24141 ų
Envelope diameter envelope_diameter85.9
Shell Rg shell_rg32.89
Envelope Rg envelope_rg26.34
Shape Rg shape_rg26.55
Total Rg total_rg27.44
Total atoms total_atoms3334
Residues n_residues436
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 dmax86.8
Rg (real space) rg_real27.64
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real3.9750e+07
I(0) uncertainty (real space) i0_real_error5.1510e+05
Rg (reciprocal space) rg_reciprocal27.62
I(0) (reciprocal space) i0_reciprocal39750000.0000
Solution quality estimate total_estimate0.8926
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary23.9
Skewness Skewness skewness0.299
Kurtosis Kurtosis kurtosis-0.699
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9817000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.921; Smooth: 0.883

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4glaa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.2 — Lysozyme-like
Superfamily Superfamily superfamilyd.2.1 — Lysozyme-like
Family Family familyd.2.1.2 — C-type lysozyme
Domain ID domain_idd4glab_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.2 — Lysozyme-like
Superfamily Superfamily superfamilyd.2.1 — Lysozyme-like
Family Family familyd.2.1.2 — C-type lysozyme

CATH v4.4 (4 domains)

Domain ID domain_id4glaA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10
Domain ID domain_id4glaB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10
Domain ID domain_id4glaC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins
Domain ID domain_id4glaD00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins

8. Citations (1)

9. Files and Curves (10)