1axt

IMMUNE VERSUS NATURAL SELECTION: ANTIBODY ALDOLASES WITH THE RATES OF NATURAL ENZYMES

Method: X-RAY DIFFRACTION Dmax: 82.9 Å Quality: EXCELLENT

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

IMMUNOGLOBULIN IGG2A

OrganismNot specified

UniProt P01865

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 1–100 Fragment:;FAB' FRAGMENT 33F12 ; IMMUNOGLOBULIN IGG2A × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.4;PROTEIN WAS CRYSTALLIZED FROM 18% PEG 4000, 10% ISOPROPANOL, 100 MM HEPES, PH 7.4. Resolution 2.15 Å R-free 0.317

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.

31 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCAM_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 119–218; UniProt 1–100

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 1axt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1axt
Deposition date deposition_date1997-10-20
Structure title titleIMMUNE VERSUS NATURAL SELECTION: ANTIBODY ALDOLASES WITH THE RATES OF NATURAL ENZYMES
Keywords keywords;IMMUNOGLOBULIN, ANTIBODY FAB', CATALYST, ALDOLASE REACTION ;; IMMUNOGLOBULIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.50
Radius of gyration Rg (electron density) rg_electron24.50
Forward intensity I(0) i038274600.00
Molecular weight molecular_weight47583.0 kDa
Excluded volume excluded_volume59394 ų
Envelope volume envelope_volume72446 ų
Hydration-shell volume shell_volume24937 ų
Envelope diameter envelope_diameter82.6
Shell Rg shell_rg31.31
Envelope Rg envelope_rg24.13
Shape Rg shape_rg24.49
Total Rg total_rg25.30
Total atoms total_atoms3350
Residues n_residues434
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 dmax82.9
Rg (real space) rg_real25.47
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real3.8270e+07
I(0) uncertainty (real space) i0_real_error5.6290e+05
Rg (reciprocal space) rg_reciprocal25.49
I(0) (reciprocal space) i0_reciprocal38270000.0000
Solution quality estimate total_estimate0.9020
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.1
Skewness Skewness skewness0.256
Kurtosis Kurtosis kurtosis-0.536
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6732000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.925; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1axth1
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_idd1axth2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd1axtl1
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_idd1axtl2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)

CATH v4.4 (4 domains)

Domain ID domain_id1axtH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1axtH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1axtL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1axtL02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)