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9e96

WEEV CBA87 VLP in complex with human PCDH10-EC1

Method: ELECTRON MICROSCOPY Dmax: 210.5 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Structural polyprotein

Western equine encephalitis virus

UniProt Q1W679

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 × 16 PDB declaration: 16-meric（16） Consistent with protein copy count Chain A； UniProt 798–1236 Chain B； UniProt 330–737 Chain F； UniProt 798–1236 Chain G； UniProt 330–737 Chain J； UniProt 798–1236 Chain K； UniProt 330–737 Chain N； UniProt 798–1236 Chain O； UniProt 330–737 Not recorded Capsid protein × 4 （P13897） Protocadherin-10 × 4 （Q9P2E7） ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 4.05 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 9E96 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8DAN CryoEM structure of Western equine encephalitis virus VLP in complex with the avian MXRA8 receptor Deposited 2022-06-13 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 798–1235（438 aa）
Chain B 321–735（415 aa）
Chain D 798–1235（438 aa）
Chain E 321–735（415 aa）
Chain G 798–1235（438 aa）
Chain H 321–735（415 aa）
Chain J 798–1235（438 aa）
Chain K 321–735（415 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.74 Å
8DAQ CryoEM structure of Western equine encephalitis virus VLP Deposited 2022-06-13 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric
Chain A 798–1235（438 aa）
Chain B 321–735（415 aa）
Chain C 798–1235（438 aa）
Chain D 321–735（415 aa）
Chain E 798–1235（438 aa）
Chain F 321–735（415 aa）
Chain G 798–1235（438 aa）
Chain H 321–735（415 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.35 Å
8SQN CryoEM structure of Western equine encephalitis virus VLP in complex with the chimeric Du-D1-Mo-D2 MXRA8 receptor Deposited 2023-05-04 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric
Chain B 798–1235（438 aa） Fragment：UNP residues 798-1235
Chain D 321–735（415 aa） Fragment：UNP residues 321-735
Chain F 798–1235（438 aa） Fragment：UNP residues 798-1235
Chain H 321–735（415 aa） Fragment：UNP residues 321-735
Chain J 798–1235（438 aa） Fragment：UNP residues 798-1235
Chain L 321–735（415 aa） Fragment：UNP residues 321-735
Chain N 798–1235（438 aa） Fragment：UNP residues 798-1235
Chain P 321–735（415 aa） Fragment：UNP residues 321-735
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.89 Å
9DQV Structure of western equine encephalitis virus CBA87 VLP in complex with human PCDH10 EC1 Deposited 2024-09-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-meric
Chain B 320–722（403 aa）
Chain E 320–722（403 aa）
Chain H 320–722（403 aa）
Chain K 320–722（403 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
9DQX Structure of western equine encephalitis virus CBA87 VLP Deposited 2024-09-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric
Chain A 798–1234（437 aa） Fragment：UNP residues 798-1235
Chain B 320–725（406 aa）
Chain D 798–1234（437 aa） Fragment：UNP residues 798-1235
Chain E 320–725（406 aa）
Chain G 798–1234（437 aa） Fragment：UNP residues 798-1235
Chain H 320–725（406 aa）
Chain J 798–1234（437 aa） Fragment：UNP residues 798-1235
Chain K 320–725（406 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q1W679_WEEV
Isoform —
PDB entities 1, 2
Chains and sequence ranges Author chain A； PDBConstruct 1–439； UniProt 798–1236 Author chain F； PDBConstruct 1–439； UniProt 798–1236 Author chain J； PDBConstruct 1–439； UniProt 798–1236 Author chain N； PDBConstruct 1–439； UniProt 798–1236 Author chain B； PDBConstruct 1–408； UniProt 330–737 Author chain G； PDBConstruct 1–408； UniProt 330–737 Author chain K； PDBConstruct 1–408； UniProt 330–737 Author chain O； PDBConstruct 1–408； UniProt 330–737

Capsid protein

Western equine encephalitis virus

UniProt P13897

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 × 16 PDB declaration: 16-meric（16） Consistent with protein copy count Chain E； UniProt 107–259 Chain I； UniProt 107–259 Chain M； UniProt 107–259 Chain R； UniProt 107–259 Not recorded Structural polyprotein × 4 （Q1W679） Structural polyprotein × 4 （Q1W679） Protocadherin-10 × 4 （Q9P2E7） ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 4.05 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 9E96 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8DEC Cryo-EM Structure of Western Equine Encephalitis Virus Deposited 2022-06-20 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 720 PDB declaration: 720-meric
Chain A 798–1236（439 aa）
Chain B 320–737（418 aa）
Chain E 1–259（259 aa）
Chain F 798–1236（439 aa）
Chain G 320–737（418 aa）
Chain I 1–259（259 aa）
Chain J 798–1236（439 aa）
Chain K 320–737（418 aa）
Chain M 1–259（259 aa）
Chain N 798–1236（439 aa）
Chain O 320–737（418 aa）
Chain R 1–259（259 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.70 Å
8DEC Cryo-EM Structure of Western Equine Encephalitis Virus Deposited 2022-06-20 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 798–1236（439 aa）
Chain B 320–737（418 aa）
Chain E 1–259（259 aa）
Chain F 798–1236（439 aa）
Chain G 320–737（418 aa）
Chain I 1–259（259 aa）
Chain J 798–1236（439 aa）
Chain K 320–737（418 aa）
Chain M 1–259（259 aa）
Chain N 798–1236（439 aa）
Chain O 320–737（418 aa）
Chain R 1–259（259 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.70 Å
8DEC Cryo-EM Structure of Western Equine Encephalitis Virus Deposited 2022-06-20 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric
Chain A 798–1236（439 aa）
Chain B 320–737（418 aa）
Chain E 1–259（259 aa）
Chain F 798–1236（439 aa）
Chain G 320–737（418 aa）
Chain I 1–259（259 aa）
Chain J 798–1236（439 aa）
Chain K 320–737（418 aa）
Chain M 1–259（259 aa）
Chain N 798–1236（439 aa）
Chain O 320–737（418 aa）
Chain R 1–259（259 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.70 Å
8DEC Cryo-EM Structure of Western Equine Encephalitis Virus Deposited 2022-06-20 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 72 PDB declaration: 72-meric
Chain A 798–1236（439 aa）
Chain B 320–737（418 aa）
Chain E 1–259（259 aa）
Chain F 798–1236（439 aa）
Chain G 320–737（418 aa）
Chain I 1–259（259 aa）
Chain J 798–1236（439 aa）
Chain K 320–737（418 aa）
Chain M 1–259（259 aa）
Chain N 798–1236（439 aa）
Chain O 320–737（418 aa）
Chain R 1–259（259 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.70 Å
8DEC Cryo-EM Structure of Western Equine Encephalitis Virus Deposited 2022-06-20 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 5 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 798–1236（439 aa）
Chain B 320–737（418 aa）
Chain E 1–259（259 aa）
Chain F 798–1236（439 aa）
Chain G 320–737（418 aa）
Chain I 1–259（259 aa）
Chain J 798–1236（439 aa）
Chain K 320–737（418 aa）
Chain M 1–259（259 aa）
Chain N 798–1236（439 aa）
Chain O 320–737（418 aa）
Chain R 1–259（259 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.70 Å
8DED Cryo-EM Structure of Western Equine Encephalitis Virus VLP in complex with SKW19 fab Deposited 2022-06-20 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric
Chain A 798–1236（439 aa）
Chain B 320–737（418 aa）
Chain F 798–1236（439 aa）
Chain G 320–737（418 aa）
Chain J 798–1236（439 aa）
Chain K 320–737（418 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.10 Å
8DEE Asymmetric Unit of Western Equine Encephalitis Virus Deposited 2022-06-20 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 798–1236（439 aa）
Chain B 320–737（418 aa）
Chain E 1–259（259 aa）
Chain F 798–1236（439 aa）
Chain G 320–737（418 aa）
Chain I 1–259（259 aa）
Chain J 798–1236（439 aa）
Chain K 320–737（418 aa）
Chain M 1–259（259 aa）
Chain N 798–1236（439 aa）
Chain O 320–737（418 aa）
Chain R 1–259（259 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
8DEF Cryo-EM Structure of Western Equine Encephalitis Virus VLP in complex with SKW24 fab Deposited 2022-06-20 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric
Chain A 798–1236（439 aa）
Chain B 320–737（418 aa）
Chain F 798–1236（439 aa）
Chain G 320–737（418 aa）
Chain J 798–1236（439 aa）
Chain K 320–737（418 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.20 Å
8DUL Cryo-EM Structure of Antibody SKT05 in complex with Western Equine Encephalitis Virus spike (local refinement from VLP particles) Deposited 2022-07-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric
Chain A 738–1226（489 aa）
Chain B 330–737（408 aa）
Chain F 738–1226（489 aa）
Chain G 330–737（408 aa）
Chain J 738–1226（489 aa）
Chain K 330–737（408 aa）
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 4.17 Å
8DUN Cryo-EM Structure of Antibody SKW11 in complex with Western Equine Encephalitis Virus spike (local refinement from VLP particles) Deposited 2022-07-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 738–1226（489 aa）
Chain B 330–737（408 aa）
Chain F 738–1226（489 aa）
Chain G 330–737（408 aa）
Chain J 738–1226（489 aa）
Chain K 330–737（408 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 5.84 Å
9DQV Structure of western equine encephalitis virus CBA87 VLP in complex with human PCDH10 EC1 Deposited 2024-09-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-meric
Chain C 97–259（163 aa）
Chain F 97–259（163 aa）
Chain I 97–259（163 aa）
Chain L 97–259（163 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
9DQX Structure of western equine encephalitis virus CBA87 VLP Deposited 2024-09-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric
Chain C 97–259（163 aa）
Chain F 97–259（163 aa）
Chain I 97–259（163 aa）
Chain L 97–259（163 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
9DQY Structure of western equine encephalitis virus Imperial 181 VLP in complex with house sparrow PCDH10 EC1 Deposited 2024-09-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric
Chain A 798–1231（434 aa）
Chain C 798–1231（434 aa）
Chain E 798–1231（434 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
9DQZ Structure of western equine encephalitis virus McMillan VLP in complex with human VLDLR Deposited 2024-09-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-meric
Chain C 102–259（158 aa）
Chain F 102–259（158 aa）
Chain I 102–259（158 aa）
Chain L 102–259（158 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 CA CALCIUM ION × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å
9E9Y WEEV McMillan VLP in complex with VLDLR LA(1-2) Deposited 2024-11-09 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-meric
Chain A 798–1236（439 aa）
Chain C 798–1236（439 aa）
Chain E 107–259（153 aa）
Chain F 107–259（153 aa）
Chain G 798–1236（439 aa）
Chain I 107–259（153 aa）
Chain J 798–1236（439 aa）
Chain L 107–259（153 aa）
Not recorded CA CALCIUM ION × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.96 Å
9E9Z SINV-WEEV Fleming in complex with VLDLR LA(1-2) Deposited 2024-11-09 Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-meric
Chain E 107–259（153 aa）
Chain F 107–259（153 aa）
Chain I 107–259（153 aa）
Chain L 107–259（153 aa）
Not recorded CA CALCIUM ION × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.95 Å
9L99 Structure of Western equine encephalitis virus McMillan strain in complex with VLDLR LA1-2 Deposited 2024-12-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain A 798–1208（411 aa）
Chain B 321–689（369 aa）
Chain G 798–1208（411 aa）
Chain H 321–689（369 aa）
Not recorded CA CALCIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
9L9A Structure of Western equine encephalitis virus McMillan strain in complex with VLDLR LA2-3 Deposited 2024-12-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain A 798–1208（411 aa）
Chain B 321–689（369 aa）
Chain G 798–1208（411 aa）
Chain H 321–689（369 aa）
Not recorded CA CALCIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 Å
9UIH CryoEM structure of Western equine encephalitis virus California VLP Deposited 2025-04-15 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 798–1236（439 aa）
Chain B 320–737（418 aa）
Chain C 798–1236（439 aa）
Chain D 320–737（418 aa）
Chain E 798–1236（439 aa）
Chain F 320–737（418 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.05 Å
9UIO CryoEM structure of Western equine encephalitis virus California VLP in complex with VLDLR-LA1-3 Deposited 2025-04-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric
Chain A 798–1236（439 aa）
Chain B 320–737（418 aa）
Chain C 798–1236（439 aa）
Chain D 320–737（418 aa）
Chain E 798–1236（439 aa）
Chain F 320–737（418 aa）
Not recorded CA CALCIUM ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.03 Å
9WSL CryoEM structure of Western equine encephalitis virus California VLP in complex with VLDLR-LBD Deposited 2025-09-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric
Chain A 798–1236（439 aa）
Chain B 320–737（418 aa）
Chain C 798–1236（439 aa）
Chain D 320–737（418 aa）
Chain E 798–1236（439 aa）
Chain F 320–737（418 aa）
Not recorded CA CALCIUM ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.27 Å

17 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLS_WEEV
Isoform —
PDB entities 3
Chains and sequence ranges Author chain E； PDBConstruct 1–153； UniProt 107–259 Author chain I； PDBConstruct 1–153； UniProt 107–259 Author chain M； PDBConstruct 1–153； UniProt 107–259 Author chain R； PDBConstruct 1–153； UniProt 107–259

Protocadherin-10

Homo sapiens

UniProt Q9P2E7

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 × 16 PDB declaration: 16-meric（16） Consistent with protein copy count Chain H； UniProt 19–122 Chain L； UniProt 19–122 Chain P； UniProt 19–122 Chain Q； UniProt 19–122 Not recorded Structural polyprotein × 4 （Q1W679） Structural polyprotein × 4 （Q1W679） Capsid protein × 4 （P13897） ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 4.05 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 9E96 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
6VFQ Crystal structure of monomeric human protocadherin 10 EC1-EC4 Deposited 2020-01-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 18–455（438 aa）
Not recorded CA CALCIUM ION × 9 MAN alpha-D-mannopyranose × 2 ACT ACETATE ION × 1 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；296 K；14% PEG 400 (v/v), 0.1M sodium acetate pH 4.6, 0.1M CaCl2, with 30% ethylene glycol (v/v) added as cryoprotectant
Resolution 2.30 Å R-free 0.237
6VFW Crystal structure of human delta protocadherin 10 EC1-EC4 Deposited 2020-01-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 18–455（438 aa）
Chain C 18–455（438 aa）
Not recorded CA CALCIUM ION × 18 MAN alpha-D-mannopyranose × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；296 K；12% (w/v) PEG 8000, 20% (v/v) ethylene glycol, 0.1M Tris-bicine buffer pH8.5, 10% 0.02 M D-glucose, 0.02 M D-mannose, 0.02 M D-galactose, 0.02 M L-fucose, 0.02 M D-xylose, 0.02 M N-acetyl-D-glucosamine with no further cryoprotection
Resolution 3.60 Å R-free 0.295
6VFW Crystal structure of human delta protocadherin 10 EC1-EC4 Deposited 2020-01-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 18–455（438 aa）
Chain D 18–455（438 aa）
Not recorded CA CALCIUM ION × 18 MAN alpha-D-mannopyranose × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；296 K；12% (w/v) PEG 8000, 20% (v/v) ethylene glycol, 0.1M Tris-bicine buffer pH8.5, 10% 0.02 M D-glucose, 0.02 M D-mannose, 0.02 M D-galactose, 0.02 M L-fucose, 0.02 M D-xylose, 0.02 M N-acetyl-D-glucosamine with no further cryoprotection
Resolution 3.60 Å R-free 0.295
6VFW Crystal structure of human delta protocadherin 10 EC1-EC4 Deposited 2020-01-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric
Chain E 18–455（438 aa）
Not recorded CA CALCIUM ION × 18 MAN alpha-D-mannopyranose × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；296 K；12% (w/v) PEG 8000, 20% (v/v) ethylene glycol, 0.1M Tris-bicine buffer pH8.5, 10% 0.02 M D-glucose, 0.02 M D-mannose, 0.02 M D-galactose, 0.02 M L-fucose, 0.02 M D-xylose, 0.02 M N-acetyl-D-glucosamine with no further cryoprotection
Resolution 3.60 Å R-free 0.295
6VG4 Human protocadherin 10 ectodomain Deposited 2020-01-07 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 18–680（663 aa）
Not recorded CA CALCIUM ION × 15 MAN alpha-D-mannopyranose × 3 TAM TRIS(HYDROXYETHYL)AMINOMETHANE × 1 CL CHLORIDE ION × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；296 K；0.22M CaCl2, 0.1M Na Acetate pH 5.0 with 30% (v/v) glycerol as cryoprotectant and glutaraldehyde (0.5% v/v) added to the reservoir after crystal formation to aid crystal stability by cross-linking
Resolution 3.30 Å R-free 0.284
9DQV Structure of western equine encephalitis virus CBA87 VLP in complex with human PCDH10 EC1 Deposited 2024-09-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-meric
Chain M 19–121（103 aa）
Chain N 19–121（103 aa）
Chain O 19–121（103 aa）
Chain P 19–121（103 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
9L1N Structure of Western equine encephalitis virus 71V1658 strain VLP in complex with human PCDH10 EC1 Deposited 2024-12-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 13 PDB declaration: 13-meric
Chain M 19–113（95 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
9L41 Structure of WEEV strain 71V1658 virus-like particles (VLPs) in complex with human PCDH10 extracellular cadherin repeats 1-2 (EC1-EC2)(3-fold region) Deposited 2024-12-19 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric
Chain R 19–114（96 aa）
Chain S 19–114（96 aa）
Chain T 19–114（96 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.99 Å

6 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PCD10_HUMAN
Isoform —
PDB entities 4
Chains and sequence ranges Author chain H； PDBConstruct 1–104； UniProt 19–122 Author chain L； PDBConstruct 1–104； UniProt 19–122 Author chain P； PDBConstruct 1–104； UniProt 19–122 Author chain Q； PDBConstruct 1–104； UniProt 19–122

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 9e96

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9e96
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9e96
Deposition date deposition_date2024-11-07
Structure title titleWEEV CBA87 VLP in complex with human PCDH10-EC1
Keywords keywordsAlphavirus Receptor, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier65.96 Å
Radius of gyration Rg (electron density) rg_electron65.18 Å
Forward intensity I(0) i03296130000.00
Molecular weight molecular_weight482690.0 kDa
Excluded volume excluded_volume603290 ų
Envelope volume envelope_volume1051200 ų
Hydration-shell volume shell_volume134290 ų
Envelope diameter envelope_diameter211.2 Å
Shell Rg shell_rg68.51 Å
Envelope Rg envelope_rg62.13 Å
Shape Rg shape_rg65.15 Å
Total Rg total_rg65.38 Å
Total atoms total_atoms33952
Residues n_residues4400
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax210.5 Å
Rg (real space) rg_real65.65 Å
Rg uncertainty (real space) rg_real_error1.81 Å
I(0) (real space) i0_real3.2960e+09
I(0) uncertainty (real space) i0_real_error6.6120e+07
Rg (reciprocal space) rg_reciprocal66.18 Å
I(0) (reciprocal space) i0_reciprocal3299000000.0000
Solution quality estimate total_estimate0.8333
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary78.9 Å
Skewness Skewness skewness0.107
Kurtosis Kurtosis kurtosis-0.631
Angular range angular_range— – 0.1200 Å−1
Current regularization parameter α current_alpha0.0003
Highest regularization parameter α highest_alpha158300000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.952; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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8. Citations (1)

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9. Files and Curves (10)