MolNFT v2 · #159624 · protein
Thioester acyl-intermediate of Apolipoprotein N-acyltransferase (Lnt)
6NWR: “Thioester acyl-intermediate of Apolipoprotein N-acyltransferase (Lnt)”. X-ray diffraction at 3.5, 1 ligand (D12). MolNFT v2 #159624 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6NWR
- Type
- protein
- Length
- 999 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.5
- Source
- Escherichia coli (strain K12)
- UniProt
- P23930
- Ligands
- D12
Structure
x-ray diffraction · resolution 3.5 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 488 | — | P23930 |
| B | — | protein | 511 | — | P23930 |
Ligands and binding sites
- D12 · Dodecane · ligand · chains B
- LMT · Dodecyl-beta-D-maltoside · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6NWR · Thioester acyl-intermediate of apolipoprotein N-acyltransferase (lnt) · the same entry in another collection · chain A against A, TM-score 1.00
- P23930 · AlphaFold monomer V2.0 prediction for apolipoprotein N-acyltransferase (P23930) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P23930
- Elsewhere: RCSB PDB 6NWR · PDBe 6NWR · UniProt P23930
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