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Structure of a thiolation-reductase di-domain from an archaeal non- ribosomal peptide synthetase
Analyse Structure of a thiolation-reductase di-domain from an archaeal non- ribosomal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VTZ
- Type
- protein
- Length
- 374 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Non-ribosomal peptide synthetase
- UniProt
- D3E027
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Non-ribosomal peptide synthetase | protein | 374 | 44% helix, 13% strand | D3E027 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 754 | 0.71 | 0.77 | 72 | empty |
Compared structures
- 6VTZ · Structure of a thiolation-reductase di-domain from an archaeal non-ribosomal peptide… · 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 D3E027
- Elsewhere: RCSB PDB 6VTZ · PDBe 6VTZ · UniProt D3E027
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