5HJ3
Crystal structure of host-primed Ebola virus GP, GPcl.
- PDB DOI: https://doi.org/10.2210/pdb5HJ3/pdb
- Classification: VIRAL PROTEIN/IMMUNE SYSTEM
- Organism(s): Ebola virus sp., Ebola virus - Zaire (1995), Homo sapiens
- Expression System: Drosophila
- Mutation(s): No 
- Deposited: 2016-01-12 Released: 2016-03-09 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 3.30 Å
- R-Value Free: 0.258 
- R-Value Work: 0.227 
- R-Value Observed: 0.228 
wwPDB Validation   3D Report Full Report
This is version 2.0 of the entry. See complete history. 
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
Envelope glycoprotein | A [auth C], E [auth G], I [auth K], M [auth O] | 179 | Ebola virus sp. | Mutation(s): 0  Gene Names: GP | |
UniProt | |||||
Find proteins for Q05320 (Zaire ebolavirus (strain Mayinga-76)) Explore Q05320  Go to UniProtKB:  Q05320 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | Q05320 | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
Envelope glycoprotein | B [auth D], F [auth H], J [auth L], N [auth P] | 136 | Ebola virus - Zaire (1995) | Mutation(s): 0  Gene Names: GP | |
UniProt | |||||
Find proteins for P87666 (Zaire ebolavirus (strain Kikwit-95)) Explore P87666  Go to UniProtKB:  P87666 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P87666 | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 3 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
KZ52 Antibody Fragment | C [auth E], G [auth I], K [auth M], O [auth A] | 226 | Homo sapiens | Mutation(s): 0  | |
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
Sequence AnnotationsExpand | |||||
|
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 4 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
KZ52 Antibody Fragment | D [auth F], H [auth J], L [auth N], P [auth B] | 217 | Homo sapiens | Mutation(s): 0  | |
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
Sequence AnnotationsExpand | |||||
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Oligosaccharides
Entity ID: 5 | |||||
---|---|---|---|---|---|
Molecule | Chains | Length | 2D Diagram | Glycosylation | 3D Interactions |
alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Q, R, S, T | 7 | N-Glycosylation | ||
Glycosylation Resources | |||||
GlyTouCan:  G23799GS GlyCosmos:  G23799GS GlyGen:  G23799GS |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 3.30 Å
- R-Value Free: 0.258 
- R-Value Work: 0.227 
- R-Value Observed: 0.228 
- Space Group: H 3
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 193.103 | α = 90 |
b = 193.103 | β = 90 |
c = 350.32 | γ = 120 |
Software Name | Purpose |
---|---|
PHENIX | refinement |
d*TREK | data scaling |
PHASER | phasing |
PDB_EXTRACT | data extraction |
d*TREK | data reduction |
Entry History 
Deposition Data
- Released Date: 2016-03-09  Deposition Author(s): Bornholdt, Z.A., Fusco, M.L., Saphire, E.O.
Revision History (Full details and data files)
- Version 1.0: 2016-03-09
Type: Initial release - Version 1.1: 2016-05-04
Changes: Database references - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Atomic model, Data collection, Derived calculations, Structure summary