MolNFT v1 · #27565 · protein
Crystal structure of E.COLI tpr-protein nlpi
1XNF · Lipoprotein nlpi: “Crystal structure of E.COLI tpr-protein nlpi”. X-ray diffraction, 7 pockets (best druggability 0.58). MolNFT v1 #27565 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1XNF
- Type
- protein
- Length
- 521 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipoprotein nlpi
- UniProt
- P39833
- Pockets
- 7 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipoprotein nlpi | protein | 259 | 76% helix, 0% strand | P39833 |
| B | Lipoprotein nlpi | protein | 262 | 74% helix, 0% strand | P39833 |
Ligands and binding sites
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 148 | 0.58 | 0.83 | 28 | empty |
| 2 | 166 | 0.48 | 0.77 | 21 | TRS |
| 3 | 170 | 0.48 | 0.76 | 25 | TRS |
| 4 | 228 | 0.47 | 0.73 | 26 | empty |
| 5 | 129 | 0.41 | 0.75 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1648 Ų buried · 26 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 1XNF · Crystal structure of E.coli TPR-protein NlpI · 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 P39833
- Elsewhere: RCSB PDB 1XNF · PDBe 1XNF · UniProt P39833
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