MolNFT v2 · #161891 · protein

Cryo-EM structure of S. cerevisiae Drs2p-Cdc50p in the autoinhibited apo form

6PSY: “Cryo-EM structure of S. cerevisiae Drs2p-Cdc50p in the autoinhibited apo form”. Electron microscopy at 2.8, 1 ligand (NAG). MolNFT v2 #161891 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6PSY
Type: protein
Length: 1,429 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.8
Source: Saccharomyces cerevisiae W303
UniProt: P39524, P25656
Ligands: NAG

Structure

electron microscopy · resolution 2.8 · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	1090	—	P39524
E	—	protein	339	—	P25656

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains E

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

Compared structures

6PSY · Cryo-EM structure of S. cerevisiae DRS2P-CDC50P in the autoinhibited apo form · the same entry in another collection · chain A against A, TM-score 1.00
P39524 · AlphaFold monomer V2.0 prediction for probable phospholipid- transporting ATPase DRS2… · a predicted model of the same protein · chain A against A, TM-score 0.99
P25656 · AlphaFold monomer V2.0 prediction for cell division control protein 50 (P25656) · a predicted model of the same protein · chain E against A, TM-score 0.97

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 P39524
Every structure of UniProt P25656
Elsewhere: RCSB PDB 6PSY · PDBe 6PSY · UniProt P39524 · UniProt P25656

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