MolNFT v2 · #204302 · protein
Cryo-EM structure of apolipoprotein N-acyltransferase Lnt from E. coli in complex with Pam3
8B0P: “Cryo-EM structure of apolipoprotein N-acyltransferase Lnt from E. coli in complex with Pam3”. Electron microscopy at 2.86, 1 ligand (IG7). MolNFT v2 #204302 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 8B0P
- Type
- protein
- Length
- 510 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.86
- Source
- Escherichia coli K-12; SYNTHETIC CONSTRUCT
- UniProt
- P23930
- Ligands
- IG7
Structure
electron microscopy · resolution 2.86 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 505 | — | P23930 |
| B | — | protein | 5 | — | — |
Ligands and binding sites
- IG7 · [(2~{S})-3-[(2~{S})-3-azanyl-2-(hexadecanoylamino)-3-oxidanylidene-propyl]sulfanyl-2-hexadecanoyloxy-propyl] hexadecanoate · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 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 8B0P · PDBe 8B0P · UniProt P23930
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