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Structure of ddn, the deazaflavin-dependent nitroreductase from mycobacterium tuberculosis involved in bioreductive activation of pa- 824
Analyse Structure of ddn, the deazaflavin-dependent nitroreductase from mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3R5L
- Type
- protein
- Length
- 116 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Deazaflavin-dependent nitroreductase
- EC
- 1.-.-.-
- UniProt
- P71854
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Deazaflavin-dependent nitroreductase (EC 1.-.-.-) | protein | 116 | 24% helix, 36% strand | P71854 |
Ligands and binding sites
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 3R5L · Structure of Ddn, the Deazaflavin-dependent nitroreductase from Mycobacterium… · 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 P71854
- Elsewhere: RCSB PDB 3R5L · PDBe 3R5L · UniProt P71854
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