E1 protein
Eastern equine encephalitis virus
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 × 20 PDB declaration: eicosameric(20) Consistent with protein copy count | Chain A; UniProt 802–1242 Chain B; UniProt 325–738 Chain D; UniProt 802–1242 Chain E; UniProt 325–738 Chain G; UniProt 802–1242 Chain H; UniProt 325–738 Chain J; UniProt 802–1242 Chain K; UniProt 325–738 | Fragment:UNP residues 802-1242 Fragment:UNP residues 325-738 | Capsid protein × 4 (W8S146) Isoform Short of Very low-density lipoprotein receptor × 8 (P98155) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CA CALCIUM ION × 12 | ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE | Resolution 3.89 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.
| Other PDB | Difference from Current Entry 8UFB | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 6XO4 CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP Deposited 2020-07-06 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer;Protein × 720 PDB declaration: 720-meric |
Chain A
802–1242(441 aa)
Chain B
325–744(420 aa)
Chain C
1–261(261 aa)
Chain D
802–1242(441 aa)
Chain E
325–744(420 aa)
Chain F
1–261(261 aa)
Chain G
802–1242(441 aa)
Chain H
325–744(420 aa)
Chain I
1–261(261 aa)
Chain J
802–1242(441 aa)
Chain K
325–744(420 aa)
Chain L
1–261(261 aa)
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE;blot time 2.5s blot force 9
|
Resolution 4.20 Å |
| 6XO4 CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP Deposited 2020-07-06 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer;Protein × 12 PDB declaration: dodecameric |
Chain A
802–1242(441 aa)
Chain B
325–744(420 aa)
Chain C
1–261(261 aa)
Chain D
802–1242(441 aa)
Chain E
325–744(420 aa)
Chain F
1–261(261 aa)
Chain G
802–1242(441 aa)
Chain H
325–744(420 aa)
Chain I
1–261(261 aa)
Chain J
802–1242(441 aa)
Chain K
325–744(420 aa)
Chain L
1–261(261 aa)
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE;blot time 2.5s blot force 9
|
Resolution 4.20 Å |
| 6XO4 CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP Deposited 2020-07-06 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein homooligomer Homooligomer;Protein × 60 PDB declaration: 60-meric |
Chain A
802–1242(441 aa)
Chain B
325–744(420 aa)
Chain C
1–261(261 aa)
Chain D
802–1242(441 aa)
Chain E
325–744(420 aa)
Chain F
1–261(261 aa)
Chain G
802–1242(441 aa)
Chain H
325–744(420 aa)
Chain I
1–261(261 aa)
Chain J
802–1242(441 aa)
Chain K
325–744(420 aa)
Chain L
1–261(261 aa)
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE;blot time 2.5s blot force 9
|
Resolution 4.20 Å |
| 6XO4 CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP Deposited 2020-07-06 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Protein homooligomer Homooligomer;Protein × 72 PDB declaration: 72-meric |
Chain A
802–1242(441 aa)
Chain B
325–744(420 aa)
Chain C
1–261(261 aa)
Chain D
802–1242(441 aa)
Chain E
325–744(420 aa)
Chain F
1–261(261 aa)
Chain G
802–1242(441 aa)
Chain H
325–744(420 aa)
Chain I
1–261(261 aa)
Chain J
802–1242(441 aa)
Chain K
325–744(420 aa)
Chain L
1–261(261 aa)
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE;blot time 2.5s blot force 9
|
Resolution 4.20 Å |
| 6XO4 CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP Deposited 2020-07-06 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 5 Protein homooligomer Homooligomer;Protein × 12 PDB declaration: dodecameric |
Chain A
802–1242(441 aa)
Chain B
325–744(420 aa)
Chain C
1–261(261 aa)
Chain D
802–1242(441 aa)
Chain E
325–744(420 aa)
Chain F
1–261(261 aa)
Chain G
802–1242(441 aa)
Chain H
325–744(420 aa)
Chain I
1–261(261 aa)
Chain J
802–1242(441 aa)
Chain K
325–744(420 aa)
Chain L
1–261(261 aa)
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE;blot time 2.5s blot force 9
|
Resolution 4.20 Å |
| 6XOB CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP with Fab EEEV-143. Deposited 2020-07-06 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 1200 PDB declaration: 1200-meric |
Chain A
802–1242(441 aa)
Chain B
325–744(420 aa)
Chain C
1–261(261 aa)
Chain D
802–1242(441 aa)
Chain E
325–744(420 aa)
Chain F
1–261(261 aa)
Chain G
802–1242(441 aa)
Chain H
325–744(420 aa)
Chain I
1–261(261 aa)
Chain J
802–1242(441 aa)
Chain K
325–744(420 aa)
Chain L
1–261(261 aa)
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE;blot time 2.5s blot force 9
|
Resolution 8.50 Å |
| 6XOB CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP with Fab EEEV-143. Deposited 2020-07-06 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer;Protein × 20 PDB declaration: eicosameric |
Chain A
802–1242(441 aa)
Chain B
325–744(420 aa)
Chain C
1–261(261 aa)
Chain D
802–1242(441 aa)
Chain E
325–744(420 aa)
Chain F
1–261(261 aa)
Chain G
802–1242(441 aa)
Chain H
325–744(420 aa)
Chain I
1–261(261 aa)
Chain J
802–1242(441 aa)
Chain K
325–744(420 aa)
Chain L
1–261(261 aa)
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE;blot time 2.5s blot force 9
|
Resolution 8.50 Å |
| 6XOB CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP with Fab EEEV-143. Deposited 2020-07-06 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein heterocomplex Heteromer;Protein × 100 PDB declaration: 100-meric |
Chain A
802–1242(441 aa)
Chain B
325–744(420 aa)
Chain C
1–261(261 aa)
Chain D
802–1242(441 aa)
Chain E
325–744(420 aa)
Chain F
1–261(261 aa)
Chain G
802–1242(441 aa)
Chain H
325–744(420 aa)
Chain I
1–261(261 aa)
Chain J
802–1242(441 aa)
Chain K
325–744(420 aa)
Chain L
1–261(261 aa)
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE;blot time 2.5s blot force 9
|
Resolution 8.50 Å |
| 6XOB CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP with Fab EEEV-143. Deposited 2020-07-06 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Protein heterocomplex Heteromer;Protein × 120 PDB declaration: 120-meric |
Chain A
802–1242(441 aa)
Chain B
325–744(420 aa)
Chain C
1–261(261 aa)
Chain D
802–1242(441 aa)
Chain E
325–744(420 aa)
Chain F
1–261(261 aa)
Chain G
802–1242(441 aa)
Chain H
325–744(420 aa)
Chain I
1–261(261 aa)
Chain J
802–1242(441 aa)
Chain K
325–744(420 aa)
Chain L
1–261(261 aa)
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE;blot time 2.5s blot force 9
|
Resolution 8.50 Å |
| 6XOB CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP with Fab EEEV-143. Deposited 2020-07-06 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 5 Protein heterocomplex Heteromer;Protein × 20 PDB declaration: eicosameric |
Chain A
802–1242(441 aa)
Chain B
325–744(420 aa)
Chain C
1–261(261 aa)
Chain D
802–1242(441 aa)
Chain E
325–744(420 aa)
Chain F
1–261(261 aa)
Chain G
802–1242(441 aa)
Chain H
325–744(420 aa)
Chain I
1–261(261 aa)
Chain J
802–1242(441 aa)
Chain K
325–744(420 aa)
Chain L
1–261(261 aa)
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE;blot time 2.5s blot force 9
|
Resolution 8.50 Å |
| 8DWO Cryo-EM Structure of Eastern Equine Encephalitis Virus in complex with SKE26 Fab Deposited 2022-08-01 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 12 PDB declaration: dodecameric |
Chain A
802–1242(441 aa)
Chain B
325–744(420 aa)
Chain F
802–1242(441 aa)
Chain G
325–744(420 aa)
Chain J
802–1242(441 aa)
Chain K
325–744(420 aa)
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.50 Å |
| 8UA4 Structure of eastern equine encephalitis virus VLP in complex with VLDLR LA1 Deposited 2023-09-20 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 17 PDB declaration: heptadecameric |
Chain A
802–1242(441 aa)
Chain B
325–744(420 aa)
Chain C
1–261(261 aa)
Chain D
802–1242(441 aa)
Chain E
325–744(420 aa)
Chain F
1–261(261 aa)
Chain G
802–1242(441 aa)
Chain H
325–744(420 aa)
Chain I
1–261(261 aa)
Chain J
802–1242(441 aa)
Chain K
325–744(420 aa)
Chain L
1–261(261 aa)
|
Mutation:K67N Mutation:K67N Mutation:K67N Mutation:K67N | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 CA CALCIUM ION × 1 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.2
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.58 Å |
| 8UA9 Structure of eastern equine encephalitis virus VLP unliganded quasi-threefold spike protein Deposited 2023-09-20 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 16 PDB declaration: hexadecameric |
Chain A
802–1242(441 aa)
Chain B
325–742(418 aa)
Fragment:UNP residues 325-744
Chain D
1–261(261 aa)
Chain E
802–1242(441 aa)
Chain F
325–742(418 aa)
Fragment:UNP residues 325-744
Chain H
1–261(261 aa)
Chain I
802–1242(441 aa)
Chain J
325–742(418 aa)
Fragment:UNP residues 325-744
Chain L
1–261(261 aa)
Chain M
802–1242(441 aa)
Chain N
325–742(418 aa)
Fragment:UNP residues 325-744
Chain P
1–261(261 aa)
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.2
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.00 Å |
| 8UFA Eastern equine encephalitis virus (PE-6) VLP (asymmetric unit) Deposited 2023-10-04 | Different oligomeric state Different ligand/ion Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 12 PDB declaration: dodecameric |
Chain A
802–1242(441 aa)
Fragment:UNP residues 802-1242
Chain B
325–738(414 aa)
Fragment:UNP residues 325-738
Chain D
802–1242(441 aa)
Fragment:UNP residues 802-1242
Chain E
325–738(414 aa)
Fragment:UNP residues 325-738
Chain G
802–1242(441 aa)
Fragment:UNP residues 802-1242
Chain H
325–738(414 aa)
Fragment:UNP residues 325-738
Chain J
802–1242(441 aa)
Fragment:UNP residues 802-1242
Chain K
325–738(414 aa)
Fragment:UNP residues 325-738
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.86 Å |
| 8UFC Eastern equine encephalitis virus (PE-6) VLP in complex with VLDLR LA(1-2) (asymmetric unit) Deposited 2023-10-04 | Different oligomeric state Different ligand/ion Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 16 PDB declaration: hexadecameric |
Chain A
802–1242(441 aa)
Fragment:UNP residues 802-1242
Chain B
325–738(414 aa)
Fragment:UNP residues 325-738
Chain D
802–1242(441 aa)
Fragment:UNP residues 802-1242
Chain E
325–738(414 aa)
Fragment:UNP residues 325-738
Chain G
802–1242(441 aa)
Fragment:UNP residues 802-1242
Chain H
325–738(414 aa)
Fragment:UNP residues 325-738
Chain J
802–1242(441 aa)
Fragment:UNP residues 802-1242
Chain K
325–738(414 aa)
Fragment:UNP residues 325-738
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CA CALCIUM ION × 8 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.09 Å |
7 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | Q88678_EEEV |
| Isoform | — |
| PDB entities | 1, 2 |
| Chains and sequence ranges | Author chain A; PDBConstruct 1–441; UniProt 802–1242 Author chain D; PDBConstruct 1–441; UniProt 802–1242 Author chain G; PDBConstruct 1–441; UniProt 802–1242 Author chain J; PDBConstruct 1–441; UniProt 802–1242 Author chain B; PDBConstruct 1–414; UniProt 325–738 Author chain E; PDBConstruct 1–414; UniProt 325–738 Author chain H; PDBConstruct 1–414; UniProt 325–738 Author chain K; PDBConstruct 1–414; UniProt 325–738 |