MolNFT v1 · #83873 · protein
Structural and biochemical study of equine lentivirus receptor 1
3WVT: “Structural and biochemical study of equine lentivirus receptor 1”. X-ray diffraction. MolNFT v1 #83873 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3WVT
- Type
- protein
- Length
- 102 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q4G265
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 102 | — | Q4G265 |
Compared structures
- 3WVT · Structural and biochemical study of equine lentivirus receptor 1 · the same entry in another collection · chain A against A, TM-score 1.00
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 Q4G265
- Elsewhere: RCSB PDB 3WVT · PDBe 3WVT · UniProt Q4G265
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