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The structure of human CHMP3 (residues 8 - 222).

Analyse The structure of human CHMP3 (residues 8 - 222). in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FRT
Type: protein
Length: 283 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Charged multivesicular body protein 3
UniProt: Q9Y3E7
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Charged multivesicular body protein 3	protein	141	81% helix, 0% strand	Q9Y3E7
B	Charged multivesicular body protein 3	protein	142	80% helix, 0% strand	Q9Y3E7

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	91	0.56	0.86	25	empty

Interfaces

1 interface between chains.

A–B · 532 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

3FRT · The structure of human CHMP3 (residues 8 - 222). · the same entry in another collection · chain A against A, TM-score 1.00
Q9Y3E7 · AlphaFold monomer V2.0 prediction for charged multivesicular body protein 3 (Q9Y3E7) · a predicted model of the same protein · chain A 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 Q9Y3E7
Elsewhere: RCSB PDB 3FRT · PDBe 3FRT · UniProt Q9Y3E7

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