Research workbench

Human GID4 bound to a PHE/N-peptide

Analyse Human GID4 bound to a PHE/N-peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7Q50
Type: protein
Length: 177 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucose-induced degradation protein 4 homolog; Fdvswfmg peptide
UniProt: Q8IVV7
Pockets: 1 · best druggability 0.55

Structure

x-ray diffraction · 2 distinct chains · 12% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glucose-induced degradation protein 4 homolog	protein	170	13% helix, 45% strand	Q8IVV7
B	Fdvswfmg peptide	protein	7	0% helix, 0% strand	—

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	154	0.55	0.80	28	empty

Interfaces

1 interface between chains.

A–B · 558 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

7Q50 · human Gid4 bound to a Phe/N-peptide · the same entry in another collection · chain A against A, TM-score 1.00
Q8IVV7 · AlphaFold monomer V2.0 prediction for glucose-induced degradation protein 4 homolog… · 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 Q8IVV7
Elsewhere: RCSB PDB 7Q50 · PDBe 7Q50 · UniProt Q8IVV7

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