Research workbench
Crystal structure of reductase (R) domain of non-ribosomal peptide synthetase from mycobacterium tuberculosis
Analyse Crystal structure of reductase (R) domain of non-ribosomal peptide synthetase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DQV
- Type
- protein
- Length
- 428 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable peptide synthetase nrp (peptide synthase)
- EC
- 6.-.-.-
- UniProt
- Q10896
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable peptide synthetase nrp (peptide synthase) (EC 6.-.-.-) | protein | 428 | 42% helix, 15% strand | Q10896 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 578 | 0.66 | 0.76 | 55 | empty |
| 2 | 216 | 0.55 | 0.78 | 27 | empty |
| 3 | 80 | 0.30 | 0.73 | 20 | empty |
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 4DQV · Crystal structure of reductase (R) domain of non-ribosomal peptide synthetase from… · 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 Q10896
- Elsewhere: RCSB PDB 4DQV · PDBe 4DQV · UniProt Q10896
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