MolNFT v1 · #54196 · protein
Crystal structure of the epimerization domain from the initiation module of tyrocidine biosynthesis
2XHG · Tyrocidine synthetase a: “Crystal structure of the epimerization domain from the initiation module of tyrocidine biosynthesis”. X-ray diffraction, 1 ligand (NA), 3 pockets (best druggability 0.80). MolNFT v1 #54196 on GenesisL1: 3D…
- 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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