Research workbench
Crystal structure of vancomycin aglycon
Analyse Crystal structure of vancomycin aglycon in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GHG
- Type
- protein
- Length
- 28 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vancomycin aglycon
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Vancomycin aglycon | protein | 7 | 0% helix, 14% strand | — |
Ligands and binding sites
- ACY · Acetic acid · additive · 4 copies · chains A, B, C, D
- DMS · Dimethyl sulfoxide · additive · 2 copies · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 189 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 186 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 17 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (nonstandard).
Compared structures
- 1GHG · Crystal structure of vancomycin aglycon · 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
- Elsewhere: RCSB PDB 1GHG · PDBe 1GHG
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