MolNFT v1 · #43768 · protein
Backbone 1H, 13C, and 15N chemical shift assignments for the catalytic domain of B. anthracis srtd
2LN7 · Lpxtg-site transpeptidase family protein: “Backbone 1H, 13C, and 15N chemical shift assignments for the catalytic domain of B. anthracis srtd”. Solution nmr, 2 pockets (best druggability 0.69). MolNFT v1 #43768 on GenesisL1: 3D…
- PDB
- 2LN7
- Type
- protein
- Length
- 147 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lpxtg-site transpeptidase family protein
- UniProt
- Q81KD1
- Pockets
- 2 · best druggability 0.69
Structure
solution nmr · 1 distinct chain · 5% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lpxtg-site transpeptidase family protein | protein | 147 | 5% helix, 44% strand | Q81KD1 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 299 | 0.69 | 0.83 | 33 | empty |
| 2 | 115 | 0.53 | 0.82 | 24 | empty |
Compared structures
- 2LN7 · Backbone 1H, 13C, and 15N Chemical Shift Assignments for the catalytic domain of B.… · 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 Q81KD1
- Elsewhere: RCSB PDB 2LN7 · PDBe 2LN7 · UniProt Q81KD1
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