Research workbench
Backbone modifications in the protein GB1 helix: beta-3-ALA24, beta-3- LYS28, beta-3-GLN32, beta-3-ASP36
Analyse Backbone modifications in the protein GB1 helix: beta-3-ALA24, beta-3- LYS28… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OZA
- Type
- protein
- Length
- 56 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Streptococcal protein GB1 backbone modified variant: beta- 3-ALA24, beta-3-LYS28…
- Ligands
- NH2
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Streptococcal protein GB1 backbone modified variant: beta- 3-ALA24, beta-3-LYS28, beta-3-GLN32, beta-3-ASP36 | protein | 56 | 32% helix, 43% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 modified (nonstandard).
Compared structures
- 4OZA · Backbone Modifications in the Protein GB1 Helix: beta-3-Ala24, beta-3-Lys28… · the same entry in another collection · chain A against A, TM-score 0.98
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 4OZA · PDBe 4OZA
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