MolNFT v1 · #104433 · protein
Crystal structure of lprf from mycobacterium bovis
4QA8 · Putative lipoprotein lprf: “Crystal structure of lprf from mycobacterium bovis”. X-ray diffraction, 1 ligand (PJZ), 1 pocket (best druggability 0.74). MolNFT v1 #104433 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4QA8
- Type
- protein
- Length
- 210 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative lipoprotein lprf
- UniProt
- P65315
- Ligands
- PJZ
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative lipoprotein lprf | protein | 210 | 15% helix, 45% strand | P65315 |
Ligands and binding sites
- PJZ · (2R)-2-(dodecanoyloxy)propyl (4E,6E,8E,10E,12E)-pentadeca-4,6,8,10,12-pentaenoate · 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 | 255 | 0.74 | 0.87 | 31 | PJZ |
Compared structures
- 4QA8 · Crystal structure of LprF from Mycobacterium bovis · the same entry in another collection · chain A against A, TM-score 1.00
- P65315 · AlphaFold monomer V2.0 prediction for putative diacylated glycolipid transporter lprf… · 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 P65315
- Elsewhere: RCSB PDB 4QA8 · PDBe 4QA8 · UniProt P65315
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.