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Truncated mitofusin-1, GDP-bound

Analyse Truncated mitofusin-1, GDP-bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5GOE
Type: protein
Length: 384 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitofusin-1
EC: 3.6.5.-
UniProt: Q8IWA4
Ligands: GDP
Pockets: 3 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 62% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitofusin-1 (EC 3.6.5.-)	protein	384	62% helix, 12% strand	Q8IWA4

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A

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

Pockets

3 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	154	0.51	0.79	31	GDP
2	66	0.33	0.76	13	empty
3	71	0.30	0.74	17	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5GOE · Truncated mitofusin-1, GDP-bound · the same entry in another collection · chain A against A, TM-score 1.00
Q8IWA4 · AlphaFold monomer V2.0 prediction for mitofusin-1 (Q8IWA4) · 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 Q8IWA4
Elsewhere: RCSB PDB 5GOE · PDBe 5GOE · UniProt Q8IWA4

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