8ecz

Bovine Fab 4C1

Method: X-RAY DIFFRACTION Dmax: 115.1 Å Quality: GOOD

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

4C1 Fab light chain

Homo sapiens

UniProt P0DOY2

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 L; UniProt 16–106 Not recorded 4C1 Fab heavy chain × 1 (P0DOX5) PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293.15 K;0.1M Tris, 50% MPD, 0.2M ammonium dihydrogen phosphate Resolution 2.82 Å R-free 0.258
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 16–106 Not recorded 4C1 Fab heavy chain × 1 (P0DOX5) PO4 PHOSPHATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293.15 K;0.1M Tris, 50% MPD, 0.2M ammonium dihydrogen phosphate Resolution 2.82 Å R-free 0.258

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.

7 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGLC2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 126–216; UniProt 16–106 Author chain L; PDBConstruct 126–216; UniProt 16–106

4C1 Fab heavy chain

Homo sapiens

UniProt P0DOX5

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 H; UniProt 114–222 Not recorded 4C1 Fab light chain × 1 (P0DOY2) PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293.15 K;0.1M Tris, 50% MPD, 0.2M ammonium dihydrogen phosphate Resolution 2.82 Å R-free 0.258
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 114–222 Not recorded 4C1 Fab light chain × 1 (P0DOY2) PO4 PHOSPHATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293.15 K;0.1M Tris, 50% MPD, 0.2M ammonium dihydrogen phosphate Resolution 2.82 Å R-free 0.258

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.

105 other PDB entries and 127 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGG1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 164–272; UniProt 114–222 Author chain H; PDBConstruct 164–272; UniProt 114–222

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 8ecz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ecz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ecz
Deposition date deposition_date2022-09-02
Structure title titleBovine Fab 4C1
Keywords keywordsantibody, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.35
Radius of gyration Rg (electron density) rg_electron33.60
Forward intensity I(0) i0175598000.00
Molecular weight molecular_weight101560.0 kDa
Excluded volume excluded_volume125500 ų
Envelope volume envelope_volume175030 ų
Hydration-shell volume shell_volume44482 ų
Envelope diameter envelope_diameter118.6
Shell Rg shell_rg39.30
Envelope Rg envelope_rg33.09
Shape Rg shape_rg33.56
Total Rg total_rg34.17
Total atoms total_atoms14019
Residues n_residues943
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 dmax115.1
Rg (real space) rg_real34.30
Rg uncertainty (real space) rg_real_error1.23
I(0) (real space) i0_real1.7560e+08
I(0) uncertainty (real space) i0_real_error3.0270e+06
Rg (reciprocal space) rg_reciprocal34.33
I(0) (reciprocal space) i0_reciprocal175600000.0000
Solution quality estimate total_estimate0.8736
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.0
Skewness Skewness skewness0.304
Kurtosis Kurtosis kurtosis-0.186
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17470000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.828; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.873

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)