Research workbench
Glycoprotein B from herpes simplex virus type 1, W174R mutant, low-pH
Analyse Glycoprotein B from herpes simplex virus type 1, W174R mutant, low-pH in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NWA
- Type
- protein
- Length
- 2,430 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P06437
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 607 | — | P06437 |
| A, C | — | protein | 608 | — | P06437 |
| D | — | protein | 607 | — | P06437 |
Compared structures
- 3NWA · Glycoprotein B from Herpes simplex virus type 1, W174R mutant, low-pH · the same entry in another collection · chain B against B, 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 P06437
- Elsewhere: RCSB PDB 3NWA · PDBe 3NWA · UniProt P06437
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