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Backbone 1H, 13C, and 15N chemical shift assignments and NMR structure for potential drug target from burkholderia thailandensis E264
Analyse Backbone 1H, 13C, and 15N chemical shift assignments and NMR structure for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MRL
- Type
- protein
- Length
- 72 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q2SV23
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 72 | — | Q2SV23 |
Compared structures
- 2MRL · Backbone 1H, 13C, and 15N Chemical Shift Assignments and NMR structure for potential drug… · 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 Q2SV23
- Elsewhere: RCSB PDB 2MRL · PDBe 2MRL · UniProt Q2SV23
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