5vzx

Crystal structure of crenezumab Fab

Method: X-RAY DIFFRACTION Dmax: 117.5 Å Quality: GOOD

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

Crenezumab 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 115–227 Chain H; UniProt 115–227 Not recorded Crenezumab Fab light chain × 2 (Q0KKI6) SO4 SULFATE ION × 11 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;2.4 M ammonium sulfate, 0.1M HEPES pH 7.5 Resolution 2.50 Å R-free 0.230
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 115–227 Not recorded Crenezumab Fab light chain × 1 (Q0KKI6) SO4 SULFATE ION × 6 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;2.4 M ammonium sulfate, 0.1M HEPES pH 7.5 Resolution 2.50 Å R-free 0.230
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 115–227 Not recorded Crenezumab Fab light chain × 1 (Q0KKI6) SO4 SULFATE ION × 5 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;2.4 M ammonium sulfate, 0.1M HEPES pH 7.5 Resolution 2.50 Å R-free 0.230

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 126 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 E; PDBConstruct 108–220; UniProt 115–227 Author chain H; PDBConstruct 108–220; UniProt 115–227

Crenezumab Fab 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain I; UniProt 110–219 Chain L; UniProt 110–219 Not recorded Crenezumab Fab heavy chain × 2 (P0DOX5) SO4 SULFATE ION × 11 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;2.4 M ammonium sulfate, 0.1M HEPES pH 7.5 Resolution 2.50 Å R-free 0.230
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain L; UniProt 110–219 Not recorded Crenezumab Fab heavy chain × 1 (P0DOX5) SO4 SULFATE ION × 6 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;2.4 M ammonium sulfate, 0.1M HEPES pH 7.5 Resolution 2.50 Å R-free 0.230
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 110–219 Not recorded Crenezumab Fab heavy chain × 1 (P0DOX5) SO4 SULFATE ION × 5 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;2.4 M ammonium sulfate, 0.1M HEPES pH 7.5 Resolution 2.50 Å R-free 0.230

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 5 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 I; PDBConstruct 110–219; UniProt 110–219 Author chain L; PDBConstruct 110–219; UniProt 110–219

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 5vzx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5vzx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5vzx
Deposition date deposition_date2017-05-29
Structure title titleCrystal structure of crenezumab Fab
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_guinier29.89
Radius of gyration Rg (electron density) rg_electron28.66
Forward intensity I(0) i0153327000.00
Molecular weight molecular_weight94424.0 kDa
Excluded volume excluded_volume116730 ų
Envelope volume envelope_volume148400 ų
Hydration-shell volume shell_volume42369 ų
Envelope diameter envelope_diameter121.4
Shell Rg shell_rg36.68
Envelope Rg envelope_rg28.41
Shape Rg shape_rg28.61
Total Rg total_rg29.55
Total atoms total_atoms6621
Residues n_residues847
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 dmax117.5
Rg (real space) rg_real29.72
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real1.5330e+08
I(0) uncertainty (real space) i0_real_error2.3040e+06
Rg (reciprocal space) rg_reciprocal29.80
I(0) (reciprocal space) i0_reciprocal153300000.0000
Solution quality estimate total_estimate0.7950
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary39.9
Skewness Skewness skewness0.168
Kurtosis Kurtosis kurtosis-0.120
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha28980000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.456; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd5vzxe_
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_idd5vzxh_
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_idd5vzxi1
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_idd5vzxi2
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
Domain ID domain_idd5vzxl1
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_idd5vzxl2
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 (6 domains)

Domain ID domain_id5vzxE02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5vzxH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5vzxI01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5vzxI02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5vzxL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5vzxL02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)