1p4i

Crystal Structure of scFv against peptide GCN4

Method: X-RAY DIFFRACTION Dmax: 58.3 Å Quality: GOOD

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

ANTIBODY VARIABLE LIGHT CHAIN

Mus musculus

UniProt P01723

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 22–117 Mutation:N36S antibody variable heavy chain × 1 (P01820) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.8;293 K;ammonium sulfate, sodium citrate, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.80 Å R-free 0.260

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LV1A_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain L; PDBConstruct 7–102; UniProt 22–117

antibody variable heavy chain

Mus musculus

UniProt P01820

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 21–115 Not recorded ANTIBODY VARIABLE LIGHT CHAIN × 1 (P01723) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.8;293 K;ammonium sulfate, sodium citrate, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.80 Å R-free 0.260

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.

14 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HV44_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 2–96; UniProt 21–115

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 1p4i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1p4i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1p4i
Deposition date deposition_date2003-04-23
Structure title titleCrystal Structure of scFv against peptide GCN4
Keywords keywordspeptide binder, scFv, picomolar binder, 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_guinier18.33
Radius of gyration Rg (electron density) rg_electron17.23
Forward intensity I(0) i010300300.00
Molecular weight molecular_weight23611.0 kDa
Excluded volume excluded_volume29432 ų
Envelope volume envelope_volume33784 ų
Hydration-shell volume shell_volume16620 ų
Envelope diameter envelope_diameter59.2
Shell Rg shell_rg23.14
Envelope Rg envelope_rg17.43
Shape Rg shape_rg17.18
Total Rg total_rg18.33
Total atoms total_atoms1665
Residues n_residues222
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 dmax58.3
Rg (real space) rg_real18.24
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real1.0300e+07
I(0) uncertainty (real space) i0_real_error1.1920e+05
Rg (reciprocal space) rg_reciprocal18.26
I(0) (reciprocal space) i0_reciprocal10300000.0000
Solution quality estimate total_estimate0.8979
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.6
Skewness Skewness skewness0.199
Kurtosis Kurtosis kurtosis-0.407
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2902000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.894; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1p4ih_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd1p4il_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)

CATH v4.4 (2 domains)

Domain ID domain_id1p4iH00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1p4iL00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)