MolNFT v2 · #178788 · protein

Overall structure of the LAT1-4F2hc bound with JX-075

7DSK: “Overall structure of the LAT1-4F2hc bound with JX-075”. Electron microscopy at 2.9, 4 ligands (Y01, 3PH, HNX). MolNFT v2 #178788 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7DSK
Type: protein
Length: 935 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.9
Source: Homo sapiens
UniProt: J3KPF3, Q01650
Ligands: Y01, 3PH, HNX, NAG

Structure

electron microscopy · resolution 2.9 · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	471	—	J3KPF3
B	—	protein	464	—	Q01650

Ligands and binding sites

Y01 · Cholesterol hemisuccinate · ligand · 2 copies · chains A, B
3PH · 1,2-diacyl-glycerol-3-sn-phosphate · ligand · chains A, B
HNX · (2~{S})-2-azanyl-7-(naphthalen-1-ylmethoxy)-3,4-dihydro-1~{H}-naphthalene-2-carboxylic acid · ligand · chains B
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

7DSK · Overall structure of the LAT1-4F2HC bound with jx-075 · the same entry in another collection · chain A against A, TM-score 1.00
Q01650 · AlphaFold monomer V2.0 prediction for large neutral amino acids transporter small subunit… · a predicted model of the same protein · chain B against A, TM-score 0.90

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 J3KPF3
Every structure of UniProt Q01650
Elsewhere: RCSB PDB 7DSK · PDBe 7DSK · UniProt J3KPF3 · UniProt Q01650

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