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Solution structure of the central conserved region of human respiratory syncytial virus attachment glycoprotein G 187
Analyse Solution structure of the central conserved region of human respiratory… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KWD
- Type
- protein
- Length
- 16 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major surface glycoprotein G
- UniProt
- P20895
Structure
solution nmr · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Major surface glycoprotein G | protein | 16 | 0% helix, 0% strand | P20895 |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1KWD · Solution structure of the central conserved region of human respiratory syncytial virus… · 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 P20895
- Elsewhere: RCSB PDB 1KWD · PDBe 1KWD · UniProt P20895
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