MolNFT v1 · #13223 · protein

NMR structure of an achr-peptide (torpedo californica, alpha-subunit residues 182-202) in complex with alpha-bungarotoxin

1L4W: “NMR structure of an achr-peptide (torpedo californica, alpha-subunit residues 182-202) in complex with…”. Solution nmr. MolNFT v1 #13223 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1L4W
Type: protein
Length: 99 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-bungarotoxin; Acetylcholine receptor protein
UniProt: P60615, P02711

Structure

solution nmr · 2 distinct chains · 0% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-bungarotoxin	protein	74	0% helix, 46% strand	P60615
B	Acetylcholine receptor protein	protein	25	0% helix, 36% strand	P02711

Interfaces

1 interface between chains.

A–B · 804 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

1L4W · NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in… · the same entry in another collection · chain A against A, TM-score 1.00
P60615 · AlphaFold monomer V2.0 prediction for alpha-bungarotoxin (P60615) · a predicted model of the same protein · chain A against A, TM-score 0.80
P02711 · AlphaFold monomer V2.0 prediction for acetylcholine receptor subunit alpha (P02711) · a predicted model of the same protein · chain B against A, TM-score 0.31

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 P60615
Every structure of UniProt P02711
Elsewhere: RCSB PDB 1L4W · PDBe 1L4W · UniProt P60615 · UniProt P02711

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