MolNFT v1 · #37118 · protein
Pnra from treponema pallidum complexed with adenosine.
2FQY · Membrane lipoprotein tmpc: “Pnra from treponema pallidum complexed with adenosine.”. X-ray diffraction, 1 ligand (ADN), 1 pocket (best druggability 0.69). MolNFT v1 #37118 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 2FQY
- 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
- ADN
- Pockets
- 1 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Membrane lipoprotein tmpc | protein | 316 | 44% helix, 21% strand | P29724 |
Ligands and binding sites
- ADN · Adenosine · 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 | 86 | 0.69 | 0.94 | 25 | ADN |
Compared structures
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 2FQY · PDBe 2FQY · UniProt P29724
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