1a7r

FV FRAGMENT OF MOUSE MONOCLONAL ANTIBODY D1.3 (BALB/C, IGG1, K) VARIANT CHAIN L GLU81->ASP

Method: X-RAY DIFFRACTION Dmax: 56.6 Å Quality: EXCELLENT

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

IGG1-KAPPA D1.3 FV (LIGHT CHAIN)

Mus musculus

UniProt P01635

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 1–108 Fragment:FV FRAGMENT Mutation:E81D IGG1-KAPPA D1.3 FV (HEAVY CHAIN) × 1 (P01820) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.01 Å

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.

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

View Construct and Data Evidence
UniProt name KV5C_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain L; PDBConstruct 1–107; UniProt 1–108

IGG1-KAPPA D1.3 FV (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 133–248 Fragment:FV FRAGMENT IGG1-KAPPA D1.3 FV (LIGHT CHAIN) × 1 (P01635) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.01 Å

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 1–116; UniProt 133–248

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 1a7r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a7r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a7r
Deposition date deposition_date1998-03-16
Structure title titleFV FRAGMENT OF MOUSE MONOCLONAL ANTIBODY D1.3 (BALB/C, IGG1, K) VARIANT CHAIN L GLU81->ASP
Keywords keywordsIMMUNOGLOBULIN; IMMUNOGLOBULIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.26
Radius of gyration Rg (electron density) rg_electron17.29
Forward intensity I(0) i010903200.00
Molecular weight molecular_weight24316.0 kDa
Excluded volume excluded_volume30261 ų
Envelope volume envelope_volume33951 ų
Hydration-shell volume shell_volume16669 ų
Envelope diameter envelope_diameter57.7
Shell Rg shell_rg23.14
Envelope Rg envelope_rg17.45
Shape Rg shape_rg17.24
Total Rg total_rg18.29
Total atoms total_atoms1715
Residues n_residues223
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 dmax56.6
Rg (real space) rg_real18.18
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real1.0900e+07
I(0) uncertainty (real space) i0_real_error1.3120e+05
Rg (reciprocal space) rg_reciprocal18.20
I(0) (reciprocal space) i0_reciprocal10900000.0000
Solution quality estimate total_estimate0.9053
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.0
Skewness Skewness skewness0.209
Kurtosis Kurtosis kurtosis-0.432
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3148000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.927; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.987

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_idd1a7rh_
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_idd1a7rl_
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_id1a7rH00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1a7rL00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (3)

9. Files and Curves (10)