4gn5

OBody AM3L15 bound to hen egg-white lysozyme

Method: X-RAY DIFFRACTION Dmax: 91.7 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 D; UniProt 19–147 Fragment:UNP residues 19-147 OBody AM3L15 × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 GOL GLYCEROL × 2 ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.4;291 K;0.2 M HEPES, 5% MPEG5000, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 1.86 Å R-free 0.202
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 19–147 Fragment:UNP residues 19-147 OBody AM3L15 × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.4;291 K;0.2 M HEPES, 5% MPEG5000, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 1.86 Å R-free 0.202

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 2
Chains and sequence ranges Author chain C; PDBConstruct 1–129; UniProt 19–147 Author chain D; 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 4gn5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4gn5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4gn5
Deposition date deposition_date2012-08-16
Structure title titleOBody AM3L15 bound to hen egg-white lysozyme
Keywords keywords;beta barrel, OB-fold, protein-protein complex, novel scaffold, muraminidase, enzyme inhibition, engineered binding protein, inhibitor, DE NOVO PROTEIN-HYDROLASE complex ;; DE NOVO PROTEIN/HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.70
Radius of gyration Rg (electron density) rg_electron28.25
Forward intensity I(0) i048800100.00
Molecular weight molecular_weight53188.0 kDa
Excluded volume excluded_volume66021 ų
Envelope volume envelope_volume83061 ų
Hydration-shell volume shell_volume25151 ų
Envelope diameter envelope_diameter98.8
Shell Rg shell_rg34.47
Envelope Rg envelope_rg28.36
Shape Rg shape_rg28.27
Total Rg total_rg28.83
Total atoms total_atoms3738
Residues n_residues478
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 dmax91.7
Rg (real space) rg_real28.79
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real4.8800e+07
I(0) uncertainty (real space) i0_real_error7.3490e+05
Rg (reciprocal space) rg_reciprocal28.75
I(0) (reciprocal space) i0_reciprocal48800000.0000
Solution quality estimate total_estimate0.8839
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.0
Skewness Skewness skewness0.350
Kurtosis Kurtosis kurtosis-0.619
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14770000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.832; Smooth: 0.927

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4gn5c_
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_idd4gn5d_
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_id4gn5A00
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_id4gn5B00
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_id4gn5C00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10
Domain ID domain_id4gn5D00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)