Research workbench
Crystal structure of the epimerization domain from the initiation module of tyrocidine biosynthesis
Analyse Crystal structure of the epimerization domain from the initiation module of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XHG
- Type
- protein
- Length
- 457 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrocidine synthetase a
- Ligands
- NA
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrocidine synthetase a | protein | 457 | 39% helix, 21% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1121 | 0.80 | 0.81 | 108 | NA |
| 2 | 60 | 0.59 | 0.90 | 16 | GOL |
| 3 | 142 | 0.51 | 0.80 | 19 | GOL |
Compared structures
- 2XHG · Crystal Structure of the Epimerization Domain from the Initiation Module of Tyrocidine… · 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 2XHG · PDBe 2XHG
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