8ecv

Bovine Fab 2F12

Method: X-RAY DIFFRACTION Dmax: 153.9 Å Quality: GOOD

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

2F12 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 2F12 Fab Heavy chain × 1 (P0DOX5) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.2;293.15 K;0.2M sodium chloride, 0.1M phosphate-citrate buffer, 20% Peg6000 Resolution 1.81 Å R-free 0.261
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 16–106 Not recorded 2F12 Fab Heavy chain × 1 (P0DOX5) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.2;293.15 K;0.2M sodium chloride, 0.1M phosphate-citrate buffer, 20% Peg6000 Resolution 1.81 Å R-free 0.261

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

2F12 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 Non-standard monomer:Yes (specific site not provided by mmCIF) 2F12 Fab Light chain × 1 (P0DOY2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.2;293.15 K;0.2M sodium chloride, 0.1M phosphate-citrate buffer, 20% Peg6000 Resolution 1.81 Å R-free 0.261
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 114–222 Non-standard monomer:Yes (specific site not provided by mmCIF) 2F12 Fab Light chain × 1 (P0DOY2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.2;293.15 K;0.2M sodium chloride, 0.1M phosphate-citrate buffer, 20% Peg6000 Resolution 1.81 Å R-free 0.261

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 161–269; UniProt 114–222 Author chain H; PDBConstruct 161–269; 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 8ecv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8ecv
Deposition date deposition_date2022-09-02
Structure title titleBovine Fab 2F12
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_guinier45.28
Radius of gyration Rg (electron density) rg_electron45.44
Forward intensity I(0) i0158363000.00
Molecular weight molecular_weight100150.0 kDa
Excluded volume excluded_volume124220 ų
Envelope volume envelope_volume186280 ų
Hydration-shell volume shell_volume36083 ų
Envelope diameter envelope_diameter162.7
Shell Rg shell_rg47.02
Envelope Rg envelope_rg43.97
Shape Rg shape_rg45.39
Total Rg total_rg45.69
Total atoms total_atoms13874
Residues n_residues938
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 dmax153.9
Rg (real space) rg_real45.77
Rg uncertainty (real space) rg_real_error1.72
I(0) (real space) i0_real1.5840e+08
I(0) uncertainty (real space) i0_real_error2.8290e+06
Rg (reciprocal space) rg_reciprocal45.28
I(0) (reciprocal space) i0_reciprocal158300000.0000
Solution quality estimate total_estimate0.7701
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.2
Skewness Skewness skewness0.412
Kurtosis Kurtosis kurtosis-0.695
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8966000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.665; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.445; Smooth: 0.567

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)