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VPS4P-VTA1P complex with peptide binding to the central pore of VPS4P

Analyse VPS4P-VTA1P complex with peptide binding to the central pore of VPS4P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6BMF
Type: protein
Length: 1,407 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P52917
Ligands: ADP, BEF, ACE, MG, NH2

Structure

electron microscopy · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	277	—	P52917
B, C, D	—	protein	285	—	P52917
E	—	protein	267	—	P52917
G	—	protein	8	—	—

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains A, B, C, D, E
BEF · Beryllium trifluoride ion · ligand · 3 copies · chains A, B, C, D
ACE · Acetyl group · ligand · chains A, G
MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
NH2 · Amino group · ion · chains G

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

Compared structures

6BMF · Vps4p-Vta1p complex with peptide binding to the central pore of Vps4p · the same entry in another collection · chain G against G, 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 E against A, TM-score 0.96

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 6BMF · PDBe 6BMF · UniProt P52917

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