Research workbench
Pnra from treponema pallidum as purified from E. COLI (bound to inosine)
Analyse Pnra from treponema pallidum as purified from E. COLI (bound to inosine) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FQW
- Type
- protein
- Length
- 316 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Membrane lipoprotein tmpc
- UniProt
- P29724
- Ligands
- NOS
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Membrane lipoprotein tmpc | protein | 316 | 43% helix, 21% strand | P29724 |
Ligands and binding sites
- NOS · Inosine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 177 | 0.68 | 0.87 | 38 | NOS |
Compared structures
- 2FQW · PnrA from Treponema pallidum as purified from E. coli (bound to inosine) · the same entry in another collection · chain A against A, TM-score 1.00
- P29724 · AlphaFold monomer V2.0 prediction for membrane lipoprotein tmpc (P29724) · a predicted model of the same protein · 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 P29724
- Elsewhere: RCSB PDB 2FQW · PDBe 2FQW · UniProt P29724
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.