Research workbench
NMR structure of the mycobacterium tuberculosis lppm (RV2171) protein folded domain
Analyse NMR structure of the mycobacterium tuberculosis lppm (RV2171) protein folded… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NC8
- Type
- protein
- Length
- 171 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipoprotein lppm
- UniProt
- A0A045INR3
- Pockets
- 2 · best druggability 0.76
Structure
solution nmr · 1 distinct chain · 9% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipoprotein lppm | protein | 171 | 9% helix, 50% strand | A0A045INR3 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 112 | 0.76 | 0.95 | 32 | empty |
| 2 | 232 | 0.50 | 0.75 | 35 | empty |
Compared structures
- 2NC8 · NMR structure of the Mycobacterium tuberculosis LppM (Rv2171) protein folded domain · 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 A0A045INR3
- Elsewhere: RCSB PDB 2NC8 · PDBe 2NC8 · UniProt A0A045INR3
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