Research workbench
Crystal structures of nipah virus G attachment glycoprotein in complex with its receptor ephrin-B3
Analyse Crystal structures of nipah virus G attachment glycoprotein in complex with its… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3D12
- Type
- protein
- Length
- 1,138 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9IH62, O35393
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 428 | — | Q9IH62 |
| B, E | — | protein | 141 | — | O35393 |
Compared structures
- 3D12 · Crystal Structures of Nipah Virus G Attachment Glycoprotein in Complex with its Receptor… · the same entry in another collection · chain A against A, TM-score 1.00
- O35393 · AlphaFold monomer V2.0 prediction for ephrin-B3 (O35393) · a predicted model of the same protein · chain B against A, TM-score 0.94
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9IH62
- Every structure of UniProt O35393
- Elsewhere: RCSB PDB 3D12 · PDBe 3D12 · UniProt Q9IH62 · UniProt O35393
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