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Crystal structure of S.CEREVISIAE VPS4 in the SO4-bound state

Analyse Crystal structure of S.CEREVISIAE VPS4 in the SO4-bound state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3EIE
Type: protein
Length: 303 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vacuolar protein sorting-associated protein 4
UniProt: P52917
Ligands: SO4
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vacuolar protein sorting-associated protein 4	protein	303	50% helix, 15% strand	P52917

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	109	0.51	0.81	21	empty
2	97	0.42	0.78	18	empty

Compared structures

3EIE · Crystal Structure of S.cerevisiae Vps4 in the SO4-bound state · the same entry in another collection · chain A against A, TM-score 1.00
P52917 · AlphaFold monomer V2.0 prediction for vacuolar protein sorting- associated protein 4… · a predicted model of the same protein · chain A 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 P52917
Elsewhere: RCSB PDB 3EIE · PDBe 3EIE · UniProt P52917

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