MolNFT v1 · #185490 · protein

Cryo-EM structure of ATP8B1-CDC50A in E2P autoinhibited state

7PY4: “Cryo-EM structure of ATP8B1-CDC50A in E2P autoinhibited state”. Electron microscopy, 5 ligands (Y01, BEF, NAG). MolNFT v1 #185490 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7PY4
Type: protein
Length: 1,439 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: O43520, Q9NV96
Ligands: Y01, BEF, NAG, BMA, MG

Structure

electron microscopy · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	1112	—	O43520
B	—	protein	327	—	Q9NV96

Ligands and binding sites

Y01 · Cholesterol hemisuccinate · ligand · 4 copies · chains A, B
BEF · Beryllium trifluoride ion · ligand · chains A
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
BMA · beta-D-mannopyranose · sugar
MG · Magnesium ion · metal · chains A

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

Compared structures

7PY4 · Cryo-EM structure of ATP8B1-CDC50A in E2P autoinhibited state · the same entry in another collection · chain A against A, TM-score 1.00
O43520 · AlphaFold monomer V2.0 prediction for phospholipid-transporting ATPase ic (O43520) · a predicted model of the same protein · chain A against A, TM-score 0.94
Q9NV96 · AlphaFold monomer V2.0 prediction for cell cycle control protein 50A (Q9NV96) · a predicted model of the same protein · chain B against A, TM-score 0.93

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 O43520
Every structure of UniProt Q9NV96
Elsewhere: RCSB PDB 7PY4 · PDBe 7PY4 · UniProt O43520 · UniProt Q9NV96

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.