5vzy

Crystal structure of crenezumab Fab in complex with Abeta

Method: X-RAY DIFFRACTION Dmax: 79.3 Å Quality: EXCELLENT

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

Crenezumab Fab heavy chain,Immunoglobulin gamma-1 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain H; UniProt 115–227 Not recorded Crenezumab Fab light chain,Immunoblobulin light chain × 1 (Q0KKI6) Amyloid beta A4 protein × 1 (P05067) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.2 M magnesium chloride hexahydrate, 0.1 M Tris hydrochloride pH 8.5, 30% w/v polyethylene glycol 4000 Resolution 2.32 Å R-free 0.249

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 128 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGG1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain H; PDBConstruct 108–220; UniProt 115–227

Crenezumab Fab light chain,Immunoblobulin light chain

Homo sapiens

UniProt Q0KKI6

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain L; UniProt 110–219 Not recorded Crenezumab Fab heavy chain,Immunoglobulin gamma-1 heavy chain × 1 (P0DOX5) Amyloid beta A4 protein × 1 (P05067) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.2 M magnesium chloride hexahydrate, 0.1 M Tris hydrochloride pH 8.5, 30% w/v polyethylene glycol 4000 Resolution 2.32 Å R-free 0.249

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.

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

View Construct and Data Evidence
UniProt name Q0KKI6_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain L; PDBConstruct 110–219; UniProt 110–219

Amyloid beta A4 protein

Homo sapiens

UniProt P05067

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 682–696 Fragment:UNP residues 682-696 Crenezumab Fab heavy chain,Immunoglobulin gamma-1 heavy chain × 1 (P0DOX5) Crenezumab Fab light chain,Immunoblobulin light chain × 1 (Q0KKI6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.2 M magnesium chloride hexahydrate, 0.1 M Tris hydrochloride pH 8.5, 30% w/v polyethylene glycol 4000 Resolution 2.32 Å R-free 0.249

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.

211 other PDB entries and 282 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A4_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–15; UniProt 682–696

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 5vzy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5vzy
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5vzy
Deposition date deposition_date2017-05-29
Structure title titleCrystal structure of crenezumab Fab in complex with Abeta
Keywords keywordsImmunoglobulin, 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_guinier25.57
Radius of gyration Rg (electron density) rg_electron24.58
Forward intensity I(0) i037575300.00
Molecular weight molecular_weight46928.0 kDa
Excluded volume excluded_volume58493 ų
Envelope volume envelope_volume73184 ų
Hydration-shell volume shell_volume24978 ų
Envelope diameter envelope_diameter81.6
Shell Rg shell_rg31.68
Envelope Rg envelope_rg24.26
Shape Rg shape_rg24.56
Total Rg total_rg25.45
Total atoms total_atoms3307
Residues n_residues427
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 dmax79.3
Rg (real space) rg_real25.53
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real3.7580e+07
I(0) uncertainty (real space) i0_real_error5.5110e+05
Rg (reciprocal space) rg_reciprocal25.54
I(0) (reciprocal space) i0_reciprocal37580000.0000
Solution quality estimate total_estimate0.9143
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary78.0
Skewness Skewness skewness0.238
Kurtosis Kurtosis kurtosis-0.566
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6057000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.969; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.978

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd5vzyh_
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_idd5vzyl1
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_idd5vzyl2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.0 — automated matches

CATH v4.4 (3 domains)

Domain ID domain_id5vzyH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5vzyL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5vzyL02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)